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{{PBB|geneid=8470}}
{{PBB|geneid=8470}}
'''ArgBP2''' [[protein]], also referred to as '''Sorbin and SH3 domain-containing protein 2''' is a [[protein]] that in humans is encoded by the ''SORBS2'' [[gene]].<ref name="pmid9211900">{{vcite2 journal | vauthors = Wang B, Golemis EA, Kruh GD | title = ArgBP2, a multiple Src homology 3 domain-containing, Arg/Abl-interacting protein, is phosphorylated in v-Abl-transformed cells and localized in stress fibers and cardiocyte Z-disks | journal = The Journal of Biological Chemistry | volume = 272 | issue = 28 | pages = 17542–50 | date = Jul 1997 | pmid = 9211900 | pmc = | doi = 10.1074/jbc.272.28.17542 }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: SORBS2 sorbin and SH3 domain containing 2| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=8470| accessdate = }}</ref> ArgBP2 belongs to the a small family of adaptor proteins having sorbin homology (SOHO) domains. ArgBP2 is highly abundant in [[cardiac muscle]] cells at [[sarcomere|sarcomeric]] [[sarcomere|Z-disc]] structures, and is expressed in other cells at [[actin]] [[stress fiber]]s and the [[Cell nucleus|nucleus]].
'''ArgBP2''' [[protein]], also referred to as '''Sorbin and SH3 domain-containing protein 2''' is a [[protein]] that in humans is encoded by the ''SORBS2'' [[gene]].<ref name="pmid9211900">{{cite journal | vauthors = Wang B, Golemis EA, Kruh GD | title = ArgBP2, a multiple Src homology 3 domain-containing, Arg/Abl-interacting protein, is phosphorylated in v-Abl-transformed cells and localized in stress fibers and cardiocyte Z-disks | journal = The Journal of Biological Chemistry | volume = 272 | issue = 28 | pages = 17542–50 | date = Jul 1997 | pmid = 9211900 | pmc = | doi = 10.1074/jbc.272.28.17542 }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: SORBS2 sorbin and SH3 domain containing 2| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=8470| accessdate = }}</ref> ArgBP2 belongs to the a small family of adaptor proteins having sorbin homology (SOHO) domains. ArgBP2 is highly abundant in [[cardiac muscle]] cells at [[sarcomere|sarcomeric]] [[sarcomere|Z-disc]] structures, and is expressed in other cells at [[actin]] [[stress fiber]]s and the [[Cell nucleus|nucleus]].


==Structure==
==Structure==
ArgBP2 may exist in as many as 9 unique isoforms ranging from 52 kDa to 117 kDa (492 to 1100 amino acids).<ref name="entrez">{{cite web | title = Entrez Gene: SORBS2 sorbin and SH3 domain containing 2| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=8470| accessdate = }}</ref> ArgBP2 belongs to the a small family of adaptor proteins having sorbin homology (SOHO) domains and three [[SH3 domain]]s, which regulate cell adhesion, cytoskeletal organization and growth factor signaling; other members include [[SORBS1|CAP/ponsin]] and [[SORBS3|vinexin]].<ref name="ReferenceA">{{vcite2 journal | vauthors = Kioka N, Ueda K, Amachi T | title = Vinexin, CAP/ponsin, ArgBP2: a novel adaptor protein family regulating cytoskeletal organization and signal transduction | journal = Cell Structure and Function | volume = 27 | issue = 1 | pages = 1–7 | date = Feb 2002 | pmid = 11937713 }}</ref> The three [[SH3 domain]]s are [[C-terminus|C-terminal]], a serine-threonine rich domain<ref name="ReferenceB">{{vcite2 journal | vauthors = Wang B, Golemis EA, Kruh GD | title = ArgBP2, a multiple Src homology 3 domain-containing, Arg/Abl-interacting protein, is phosphorylated in v-Abl-transformed cells and localized in stress fibers and cardiocyte Z-disks | journal = The Journal of Biological Chemistry | volume = 272 | issue = 28 | pages = 17542–50 | date = Jul 1997 | pmid = 9211900 }}</ref> resides in the middle, and the sorbin homology (SoHo) domain is [[N-terminus|N-terminal]]. The SH3 domains interact with Arg/Abl, vinculin.<ref name="ReferenceA"/> The SOHO domain interacts with [[FLOT1|flotillin]] found in lipid rafts.<ref>{{vcite2 journal | vauthors = Kimura A, Baumann CA, Chiang SH, Saltiel AR | title = The sorbin homology domain: a motif for the targeting of proteins to lipid rafts | journal = Proceedings of the National Academy of Sciences of the United States of America | volume = 98 | issue = 16 | pages = 9098–103 | date = Jul 2001 | pmid = 11481476 | doi = 10.1073/pnas.151252898 }}</ref>
ArgBP2 may exist in as many as 9 unique isoforms ranging from 52 kDa to 117 kDa (492 to 1100 amino acids).<ref name="entrez">{{cite web | title = Entrez Gene: SORBS2 sorbin and SH3 domain containing 2| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=8470| accessdate = }}</ref> ArgBP2 belongs to the a small family of adaptor proteins having sorbin homology (SOHO) domains and three [[SH3 domain]]s, which regulate cell adhesion, cytoskeletal organization and growth factor signaling; other members include [[SORBS1|CAP/ponsin]] and [[SORBS3|vinexin]].<ref name="ReferenceA">{{cite journal | vauthors = Kioka N, Ueda K, Amachi T | title = Vinexin, CAP/ponsin, ArgBP2: a novel adaptor protein family regulating cytoskeletal organization and signal transduction | journal = Cell Structure and Function | volume = 27 | issue = 1 | pages = 1–7 | date = Feb 2002 | pmid = 11937713 }}</ref> The three [[SH3 domain]]s are [[C-terminus|C-terminal]], a serine-threonine rich domain<ref name="ReferenceB">{{cite journal | vauthors = Wang B, Golemis EA, Kruh GD | title = ArgBP2, a multiple Src homology 3 domain-containing, Arg/Abl-interacting protein, is phosphorylated in v-Abl-transformed cells and localized in stress fibers and cardiocyte Z-disks | journal = The Journal of Biological Chemistry | volume = 272 | issue = 28 | pages = 17542–50 | date = Jul 1997 | pmid = 9211900 }}</ref> resides in the middle, and the sorbin homology (SoHo) domain is [[N-terminus|N-terminal]]. The SH3 domains interact with Arg/Abl, vinculin.<ref name="ReferenceA"/> The SOHO domain interacts with [[FLOT1|flotillin]] found in lipid rafts.<ref>{{cite journal | vauthors = Kimura A, Baumann CA, Chiang SH, Saltiel AR | title = The sorbin homology domain: a motif for the targeting of proteins to lipid rafts | journal = Proceedings of the National Academy of Sciences of the United States of America | volume = 98 | issue = 16 | pages = 9098–103 | date = Jul 2001 | pmid = 11481476 | doi = 10.1073/pnas.151252898 }}</ref>


== Function ==
== Function ==
The subcellular localization of this protein in epithelial and cardiac muscle cells suggests that ArgBP2 functions as an adapter protein to assemble signaling complexes in stress fibers, and that it is a potential link between Abl family kinases and the actin cytoskeleton. ArgBP2 contains several potential Abl phosphorylation sites;<ref name="ReferenceB"/> Arg and c-Abl represent the mammalian members of the Abelson family of non-receptor protein-tyrosine kinases. In non-muscle cells, ArgBP2 bids [[Cbl gene|Cbl]] which enhances the degradation of [[ABL1|c-Abl]];<ref>{{vcite2 journal | vauthors = Soubeyran P, Barac A, Szymkiewicz I, Dikic I | title = Cbl-ArgBP2 complex mediates ubiquitination and degradation of c-Abl | journal = The Biochemical Journal | volume = 370 | issue = Pt 1 | pages = 29–34 | date = Feb 2003 | pmid = 12475393 | doi = 10.1042/BJ20021539 }}</ref> and also [[Pyk2]] which promotes cytoskeletal remodeling.<ref>{{vcite2 journal | vauthors = Haglund K, Ivankovic-Dikic I, Shimokawa N, Kruh GD, Dikic I | title = Recruitment of Pyk2 and Cbl to lipid rafts mediates signals important for actin reorganization in growing neurites | journal = Journal of Cell Science | volume = 117 | issue = Pt 12 | pages = 2557–68 | date = May 2004 | pmid = 15128873 | doi = 10.1242/jcs.01148 }}</ref> ArgBP2 binding with [[FLOT1|flotillin]] at lipid rafts may indicate a role for ArgBP2 in vesicle trafficking and signal transduction. Interestingly, [[FLOT1|flotillin]] in [[skeletal muscle]] cells exhibits a striated pattern<ref>{{vcite2 journal | vauthors = Voldstedlund M, Vinten J, Tranum-Jensen J | title = cav-p60 expression in rat muscle tissues. Distribution of caveolar proteins | journal = Cell and Tissue Research | volume = 306 | issue = 2 | pages = 265–76 | date = Nov 2001 | pmid = 11702238 | doi = 10.1007/s004410100439 }}</ref> suggesting localization to [[T-tubule]]s or [[sarcoplasmic reticulum|sarcoplasmic reticular]] cisternae, though no precise role has been determined in [[cardiac]] cells. In cardiac muscle cells, pull-down experiments discovered ArgBP2 in complex with [[Actinin, alpha 2|alpha actinin-2]], [[vinculin]], [[SPEC|spectrin]], [[paxillin]], [[Pyk2]] and [[FLOT1|flotillin]], suggesting that ArgBP2 may be involved in [[myofibril]] assembly and [[sarcomere|Z-band]] signaling in cardiomyocytes,<ref name = "Sanger_2010">{{vcite2 journal | vauthors = Sanger JM, Wang J, Gleason LM, Chowrashi P, Dube DK, Mittal B, Zhukareva V, Sanger JW | title = Arg/Abl-binding protein, a Z-body and Z-band protein, binds sarcomeric, costameric, and signaling molecules | journal = Cytoskeleton | volume = 67 | issue = 12 | pages = 808–23 | date = Dec 2010 | pmid = 20886612 | doi = 10.1002/cm.20490 }}</ref> though functional studies are necessary to elucidate specific mechanisms. ArgBP2 has been linked to hyertrophic signaling, as a potent paracrine-acting RNA molecule shown to induce [[cardiac hypertrophy]] in mice, miR-21, acts on both ArgBP2 and [[PDLIM5]] to trigger the [[cardiac hypertrophy|hypertrophic]] response.<ref>{{vcite2 journal | vauthors = Bang C, Batkai S, Dangwal S, Gupta SK, Foinquinos A, Holzmann A, Just A, Remke J, Zimmer K, Zeug A, Ponimaskin E, Schmiedl A, Yin X, Mayr M, Halder R, Fischer A, Engelhardt S, Wei Y, Schober A, Fiedler J, Thum T | title = Cardiac fibroblast-derived microRNA passenger strand-enriched exosomes mediate cardiomyocyte hypertrophy | journal = The Journal of Clinical Investigation | volume = 124 | issue = 5 | pages = 2136–46 | date = May 2014 | pmid = 24743145 | doi = 10.1172/JCI70577 }}</ref>
The subcellular localization of this protein in epithelial and cardiac muscle cells suggests that ArgBP2 functions as an adapter protein to assemble signaling complexes in stress fibers, and that it is a potential link between Abl family kinases and the actin cytoskeleton. ArgBP2 contains several potential Abl phosphorylation sites;<ref name="ReferenceB"/> Arg and c-Abl represent the mammalian members of the Abelson family of non-receptor protein-tyrosine kinases. In non-muscle cells, ArgBP2 bids [[Cbl gene|Cbl]] which enhances the degradation of [[ABL1|c-Abl]];<ref>{{cite journal | vauthors = Soubeyran P, Barac A, Szymkiewicz I, Dikic I | title = Cbl-ArgBP2 complex mediates ubiquitination and degradation of c-Abl | journal = The Biochemical Journal | volume = 370 | issue = Pt 1 | pages = 29–34 | date = Feb 2003 | pmid = 12475393 | doi = 10.1042/BJ20021539 }}</ref> and also [[Pyk2]] which promotes cytoskeletal remodeling.<ref>{{cite journal | vauthors = Haglund K, Ivankovic-Dikic I, Shimokawa N, Kruh GD, Dikic I | title = Recruitment of Pyk2 and Cbl to lipid rafts mediates signals important for actin reorganization in growing neurites | journal = Journal of Cell Science | volume = 117 | issue = Pt 12 | pages = 2557–68 | date = May 2004 | pmid = 15128873 | doi = 10.1242/jcs.01148 }}</ref> ArgBP2 binding with [[FLOT1|flotillin]] at lipid rafts may indicate a role for ArgBP2 in vesicle trafficking and signal transduction. Interestingly, [[FLOT1|flotillin]] in [[skeletal muscle]] cells exhibits a striated pattern<ref>{{cite journal | vauthors = Voldstedlund M, Vinten J, Tranum-Jensen J | title = cav-p60 expression in rat muscle tissues. Distribution of caveolar proteins | journal = Cell and Tissue Research | volume = 306 | issue = 2 | pages = 265–76 | date = Nov 2001 | pmid = 11702238 | doi = 10.1007/s004410100439 }}</ref> suggesting localization to [[T-tubule]]s or [[sarcoplasmic reticulum|sarcoplasmic reticular]] cisternae, though no precise role has been determined in [[cardiac]] cells. In cardiac muscle cells, pull-down experiments discovered ArgBP2 in complex with [[Actinin, alpha 2|alpha actinin-2]], [[vinculin]], [[SPEC|spectrin]], [[paxillin]], [[Pyk2]] and [[FLOT1|flotillin]], suggesting that ArgBP2 may be involved in [[myofibril]] assembly and [[sarcomere|Z-band]] signaling in cardiomyocytes,<ref name = "Sanger_2010">{{cite journal | vauthors = Sanger JM, Wang J, Gleason LM, Chowrashi P, Dube DK, Mittal B, Zhukareva V, Sanger JW | title = Arg/Abl-binding protein, a Z-body and Z-band protein, binds sarcomeric, costameric, and signaling molecules | journal = Cytoskeleton | volume = 67 | issue = 12 | pages = 808–23 | date = Dec 2010 | pmid = 20886612 | doi = 10.1002/cm.20490 }}</ref> though functional studies are necessary to elucidate specific mechanisms. ArgBP2 has been linked to hyertrophic signaling, as a potent paracrine-acting RNA molecule shown to induce [[cardiac hypertrophy]] in mice, miR-21, acts on both ArgBP2 and [[PDLIM5]] to trigger the [[cardiac hypertrophy|hypertrophic]] response.<ref>{{cite journal | vauthors = Bang C, Batkai S, Dangwal S, Gupta SK, Foinquinos A, Holzmann A, Just A, Remke J, Zimmer K, Zeug A, Ponimaskin E, Schmiedl A, Yin X, Mayr M, Halder R, Fischer A, Engelhardt S, Wei Y, Schober A, Fiedler J, Thum T | title = Cardiac fibroblast-derived microRNA passenger strand-enriched exosomes mediate cardiomyocyte hypertrophy | journal = The Journal of Clinical Investigation | volume = 124 | issue = 5 | pages = 2136–46 | date = May 2014 | pmid = 24743145 | doi = 10.1172/JCI70577 }}</ref>


==Clinical Significance==
==Clinical Significance==
Elevated levels of serum ArgBP2 and coordinate decreases in ArgBP2 in [[myocardium|myocardial]] tissue were detected in the very early phase from patients post-[[myocardial infarction]] who died within 7 hours of the insult.<ref>{{vcite2 journal | vauthors = Kakimoto Y, Ito S, Abiru H, Kotani H, Ozeki M, Tamaki K, Tsuruyama T | title = Sorbin and SH3 domain-containing protein 2 is released from infarcted heart in the very early phase: proteomic analysis of cardiac tissues from patients | journal = Journal of the American Heart Association | volume = 2 | issue = 6 | pages = e000565 | pmid = 24342996 | doi = 10.1161/JAHA.113.000565 }}</ref> Chromosome 4 [[chromosomal inversion|pericentric inversion]] has been observed in 10 patients, with associated [[cardiac]] defects linked to terminal 4q35.1 deletions, which may affect ''SORBS2''.<ref>{{vcite2 journal | vauthors = Maurin ML, Labrune P, Brisset S, Le Lorc'h M, Pineau D, Castel C, Romana S, Tachdjian G | title = Molecular cytogenetic characterization of a 4p15.1-pter duplication and a 4q35.1-qter deletion in a recombinant of chromosome 4 pericentric inversion | journal = American Journal of Medical Genetics. Part A | volume = 149A | issue = 2 | pages = 226–31 | date = Feb 2009 | pmid = 19161154 | doi = 10.1002/ajmg.a.32603 }}</ref>
Elevated levels of serum ArgBP2 and coordinate decreases in ArgBP2 in [[myocardium|myocardial]] tissue were detected in the very early phase from patients post-[[myocardial infarction]] who died within 7 hours of the insult.<ref>{{cite journal | vauthors = Kakimoto Y, Ito S, Abiru H, Kotani H, Ozeki M, Tamaki K, Tsuruyama T | title = Sorbin and SH3 domain-containing protein 2 is released from infarcted heart in the very early phase: proteomic analysis of cardiac tissues from patients | journal = Journal of the American Heart Association | volume = 2 | issue = 6 | pages = e000565 | pmid = 24342996 | doi = 10.1161/JAHA.113.000565 }}</ref> Chromosome 4 [[chromosomal inversion|pericentric inversion]] has been observed in 10 patients, with associated [[cardiac]] defects linked to terminal 4q35.1 deletions, which may affect ''SORBS2''.<ref>{{cite journal | vauthors = Maurin ML, Labrune P, Brisset S, Le Lorc'h M, Pineau D, Castel C, Romana S, Tachdjian G | title = Molecular cytogenetic characterization of a 4p15.1-pter duplication and a 4q35.1-qter deletion in a recombinant of chromosome 4 pericentric inversion | journal = American Journal of Medical Genetics. Part A | volume = 149A | issue = 2 | pages = 226–31 | date = Feb 2009 | pmid = 19161154 | doi = 10.1002/ajmg.a.32603 }}</ref>


== Interactions ==
== Interactions ==
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{{div col|colwidth=15em}}
{{div col|colwidth=15em}}
* [[ABL (gene)|ABL]],<ref name = pmid9211900/><ref name = pmid12475393/>
* [[ABL (gene)|ABL]],<ref name = pmid9211900/><ref name = pmid12475393/>
* [[ABL2]],<ref name = pmid9211900>{{vcite2 journal | vauthors = Wang B, Golemis EA, Kruh GD | date = Jul 1997 | title = ArgBP2, a multiple Src homology 3 domain-containing, Arg/Abl-interacting protein, is phosphorylated in v-Abl-transformed cells and localized in stress fibers and cardiocyte Z-disks | journal = J. Biol. Chem. | volume = 272 | issue = 28 | pages = 17542–50 | pmid = 9211900 | doi = }}</ref>
* [[ABL2]],<ref name = pmid9211900>{{cite journal | vauthors = Wang B, Golemis EA, Kruh GD | date = Jul 1997 | title = ArgBP2, a multiple Src homology 3 domain-containing, Arg/Abl-interacting protein, is phosphorylated in v-Abl-transformed cells and localized in stress fibers and cardiocyte Z-disks | journal = J. Biol. Chem. | volume = 272 | issue = 28 | pages = 17542–50 | pmid = 9211900 | doi = }}</ref>
* [[ACTC1]],<ref name = "Sanger_2010"/><ref>{{vcite2 journal | vauthors = Sanger JM, Wang J, Gleason LM, Chowrashi P, Dube DK, Mittal B, Zhukareva V, Sanger JW | date = Dec 2010 | title = Arg/Abl-binding protein, a Z-body and Z-band protein, binds sarcomeric, costameric, and signaling molecules | journal = Cytoskeleton (Hoboken) | volume = 67 | issue = 12 | pages = 808–23 | pmid = 20886612 | pmc = 3019100 | doi = 10.1002/cm.20490}}</ref>
* [[ACTC1]],<ref name = "Sanger_2010"/><ref>{{cite journal | vauthors = Sanger JM, Wang J, Gleason LM, Chowrashi P, Dube DK, Mittal B, Zhukareva V, Sanger JW | date = Dec 2010 | title = Arg/Abl-binding protein, a Z-body and Z-band protein, binds sarcomeric, costameric, and signaling molecules | journal = Cytoskeleton (Hoboken) | volume = 67 | issue = 12 | pages = 808–23 | pmid = 20886612 | pmc = 3019100 | doi = 10.1002/cm.20490}}</ref>
* [[CBL (gene)|CBL]],<ref name = pmid12475393>{{vcite2 journal | vauthors = Soubeyran P, Barac A, Szymkiewicz I, Dikic I | date = Feb 2003 | title = Cbl-ArgBP2 complex mediates ubiquitination and degradation of c-Abl | journal = Biochem. J. | volume = 370 | issue = Pt 1 | pages = 29–34 | pmid = 12475393 | pmc = 1223168 | doi = 10.1042/BJ20021539}}</ref><ref name = pmid15128873/>
* [[CBL (gene)|CBL]],<ref name = pmid12475393>{{cite journal | vauthors = Soubeyran P, Barac A, Szymkiewicz I, Dikic I | date = Feb 2003 | title = Cbl-ArgBP2 complex mediates ubiquitination and degradation of c-Abl | journal = Biochem. J. | volume = 370 | issue = Pt 1 | pages = 29–34 | pmid = 12475393 | pmc = 1223168 | doi = 10.1042/BJ20021539}}</ref><ref name = pmid15128873/>
* [[FLOT1]],<ref>{{vcite2 journal | vauthors = Kimura A, Baumann CA, Chiang SH, Saltiel AR | date = Jul 2001 | title = The sorbin homology domain: a motif for the targeting of proteins to lipid rafts | journal = Proc. Natl. Acad. Sci. U.S.A. | volume = 98 | issue = 16 | pages = 9098–103 | pmid = 11481476 | pmc = 55379 | doi = 10.1073/pnas.151252898}}</ref>
* [[FLOT1]],<ref>{{cite journal | vauthors = Kimura A, Baumann CA, Chiang SH, Saltiel AR | date = Jul 2001 | title = The sorbin homology domain: a motif for the targeting of proteins to lipid rafts | journal = Proc. Natl. Acad. Sci. U.S.A. | volume = 98 | issue = 16 | pages = 9098–103 | pmid = 11481476 | pmc = 55379 | doi = 10.1073/pnas.151252898}}</ref>
* [[PTK2B]],<ref name = pmid15128873>{{vcite2 journal | vauthors = Haglund K, Ivankovic-Dikic I, Shimokawa N, Kruh GD, Dikic I | date = May 2004 | title = Recruitment of Pyk2 and Cbl to lipid rafts mediates signals important for actin reorganization in growing neurites | journal = J. Cell. Sci. | volume = 117 | issue = Pt 12 | pages = 2557–68 | pmid = 15128873 | doi = 10.1242/jcs.01148}}</ref>
* [[PTK2B]],<ref name = pmid15128873>{{cite journal | vauthors = Haglund K, Ivankovic-Dikic I, Shimokawa N, Kruh GD, Dikic I | date = May 2004 | title = Recruitment of Pyk2 and Cbl to lipid rafts mediates signals important for actin reorganization in growing neurites | journal = J. Cell. Sci. | volume = 117 | issue = Pt 12 | pages = 2557–68 | pmid = 15128873 | doi = 10.1242/jcs.01148}}</ref>
* [[PLDN]],<ref>{{vcite2 journal | vauthors = Rönty M, Taivainen A, Moza M, Kruh GD, Ehler E, Carpen O | date = Oct 2005 | title = Involvement of palladin and alpha-actinin in targeting of the Abl/Arg kinase adaptor ArgBP2 to the actin cytoskeleton | journal = Exp. Cell Res. | volume = 310 | issue = 1 | pages = 88–98 | pmid = 16125169 | doi = 10.1016/j.yexcr.2005.06.026}}</ref> and
* [[PLDN]],<ref>{{cite journal | vauthors = Rönty M, Taivainen A, Moza M, Kruh GD, Ehler E, Carpen O | date = Oct 2005 | title = Involvement of palladin and alpha-actinin in targeting of the Abl/Arg kinase adaptor ArgBP2 to the actin cytoskeleton | journal = Exp. Cell Res. | volume = 310 | issue = 1 | pages = 88–98 | pmid = 16125169 | doi = 10.1016/j.yexcr.2005.06.026}}</ref> and
* [[vinculin|VCL]].<ref name = "Sanger_2010"/><ref>{{vcite2 journal | vauthors = Kioka N, Ueda K, Amachi T | date = Feb 2002 | title = Vinexin, CAP/ponsin, ArgBP2: a novel adaptor protein family regulating cytoskeletal organization and signal transduction | journal = Cell Struct. Funct. | volume = 27 | issue = 1 | pages = 1–7 | pmid = 11937713 | doi = }}</ref>
* [[vinculin|VCL]].<ref name = "Sanger_2010"/><ref>{{cite journal | vauthors = Kioka N, Ueda K, Amachi T | date = Feb 2002 | title = Vinexin, CAP/ponsin, ArgBP2: a novel adaptor protein family regulating cytoskeletal organization and signal transduction | journal = Cell Struct. Funct. | volume = 27 | issue = 1 | pages = 1–7 | pmid = 11937713 | doi = }}</ref>
{{Div col end}}
{{Div col end}}


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== Further reading ==
== Further reading ==
{{refbegin|33em}}
{{refbegin|33em}}
* {{vcite2 journal | vauthors = Kioka N | title = [A novel adaptor protein family regulating cytoskeletal organization and signal transduction--Vinexin, CAP/ponsin, ArgBP2] | journal = Seikagaku. The Journal of Japanese Biochemical Society | volume = 74 | issue = 11 | pages = 1356–60 | date = Nov 2002 | pmid = 12510380 | doi = }}
* {{cite journal | vauthors = Kioka N | title = [A novel adaptor protein family regulating cytoskeletal organization and signal transduction--Vinexin, CAP/ponsin, ArgBP2] | journal = Seikagaku. The Journal of Japanese Biochemical Society | volume = 74 | issue = 11 | pages = 1356–60 | date = Nov 2002 | pmid = 12510380 | doi = }}
* {{vcite2 journal | vauthors = Maruyama K, Sugano S | title = Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides | journal = Gene | volume = 138 | issue = 1-2 | pages = 171–4 | date = Jan 1994 | pmid = 8125298 | doi = 10.1016/0378-1119(94)90802-8 }}
* {{cite journal | vauthors = Maruyama K, Sugano S | title = Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides | journal = Gene | volume = 138 | issue = 1-2 | pages = 171–4 | date = Jan 1994 | pmid = 8125298 | doi = 10.1016/0378-1119(94)90802-8 }}
* {{vcite2 journal | vauthors = Hillier LD, Lennon G, Becker M, Bonaldo MF, Chiapelli B, Chissoe S, Dietrich N, DuBuque T, Favello A, Gish W, Hawkins M, Hultman M, Kucaba T, Lacy M, Le M, Le N, Mardis E, Moore B, Morris M, Parsons J, Prange C, Rifkin L, Rohlfing T, Schellenberg K, Bento Soares M, Tan F, Thierry-Meg J, Trevaskis E, Underwood K, Wohldman P, Waterston R, Wilson R, Marra M | title = Generation and analysis of 280,000 human expressed sequence tags | journal = Genome Research | volume = 6 | issue = 9 | pages = 807–28 | date = Sep 1996 | pmid = 8889549 | doi = 10.1101/gr.6.9.807 }}
* {{cite journal | vauthors = Hillier LD, Lennon G, Becker M, Bonaldo MF, Chiapelli B, Chissoe S, Dietrich N, DuBuque T, Favello A, Gish W, Hawkins M, Hultman M, Kucaba T, Lacy M, Le M, Le N, Mardis E, Moore B, Morris M, Parsons J, Prange C, Rifkin L, Rohlfing T, Schellenberg K, Bento Soares M, Tan F, Thierry-Meg J, Trevaskis E, Underwood K, Wohldman P, Waterston R, Wilson R, Marra M | title = Generation and analysis of 280,000 human expressed sequence tags | journal = Genome Research | volume = 6 | issue = 9 | pages = 807–28 | date = Sep 1996 | pmid = 8889549 | doi = 10.1101/gr.6.9.807 }}
* {{vcite2 journal | vauthors = Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, Suyama A, Sugano S | title = Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library | journal = Gene | volume = 200 | issue = 1-2 | pages = 149–56 | date = Oct 1997 | pmid = 9373149 | doi = 10.1016/S0378-1119(97)00411-3 }}
* {{cite journal | vauthors = Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, Suyama A, Sugano S | title = Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library | journal = Gene | volume = 200 | issue = 1-2 | pages = 149–56 | date = Oct 1997 | pmid = 9373149 | doi = 10.1016/S0378-1119(97)00411-3 }}
* {{vcite2 journal | vauthors = Kawabe H, Hata Y, Takeuchi M, Ide N, Mizoguchi A, Takai Y | title = nArgBP2, a novel neural member of ponsin/ArgBP2/vinexin family that interacts with synapse-associated protein 90/postsynaptic density-95-associated protein (SAPAP) | journal = The Journal of Biological Chemistry | volume = 274 | issue = 43 | pages = 30914–8 | date = Oct 1999 | pmid = 10521485 | doi = 10.1074/jbc.274.43.30914 }}
* {{cite journal | vauthors = Kawabe H, Hata Y, Takeuchi M, Ide N, Mizoguchi A, Takai Y | title = nArgBP2, a novel neural member of ponsin/ArgBP2/vinexin family that interacts with synapse-associated protein 90/postsynaptic density-95-associated protein (SAPAP) | journal = The Journal of Biological Chemistry | volume = 274 | issue = 43 | pages = 30914–8 | date = Oct 1999 | pmid = 10521485 | doi = 10.1074/jbc.274.43.30914 }}
* {{vcite2 journal | vauthors = Hartley JL, Temple GF, Brasch MA | title = DNA cloning using in vitro site-specific recombination | journal = Genome Research | volume = 10 | issue = 11 | pages = 1788–95 | date = Nov 2000 | pmid = 11076863 | pmc = 310948 | doi = 10.1101/gr.143000 }}
* {{cite journal | vauthors = Hartley JL, Temple GF, Brasch MA | title = DNA cloning using in vitro site-specific recombination | journal = Genome Research | volume = 10 | issue = 11 | pages = 1788–95 | date = Nov 2000 | pmid = 11076863 | pmc = 310948 | doi = 10.1101/gr.143000 }}
* {{vcite2 journal | vauthors = Wiemann S, Weil B, Wellenreuther R, Gassenhuber J, Glassl S, Ansorge W, Böcher M, Blöcker H, Bauersachs S, Blum H, Lauber J, Düsterhöft A, Beyer A, Köhrer K, Strack N, Mewes HW, Ottenwälder B, Obermaier B, Tampe J, Heubner D, Wambutt R, Korn B, Klein M, Poustka A | title = Toward a catalog of human genes and proteins: sequencing and analysis of 500 novel complete protein coding human cDNAs | journal = Genome Research | volume = 11 | issue = 3 | pages = 422–35 | date = Mar 2001 | pmid = 11230166 | pmc = 311072 | doi = 10.1101/gr.GR1547R }}
* {{cite journal | vauthors = Wiemann S, Weil B, Wellenreuther R, Gassenhuber J, Glassl S, Ansorge W, Böcher M, Blöcker H, Bauersachs S, Blum H, Lauber J, Düsterhöft A, Beyer A, Köhrer K, Strack N, Mewes HW, Ottenwälder B, Obermaier B, Tampe J, Heubner D, Wambutt R, Korn B, Klein M, Poustka A | title = Toward a catalog of human genes and proteins: sequencing and analysis of 500 novel complete protein coding human cDNAs | journal = Genome Research | volume = 11 | issue = 3 | pages = 422–35 | date = Mar 2001 | pmid = 11230166 | pmc = 311072 | doi = 10.1101/gr.GR1547R }}
* {{vcite2 journal | vauthors = Zucconi A, Dente L, Santonico E, Castagnoli L, Cesareni G | title = Selection of ligands by panning of domain libraries displayed on phage lambda reveals new potential partners of synaptojanin 1 | journal = Journal of Molecular Biology | volume = 307 | issue = 5 | pages = 1329–39 | date = Apr 2001 | pmid = 11292345 | doi = 10.1006/jmbi.2001.4572 }}
* {{cite journal | vauthors = Zucconi A, Dente L, Santonico E, Castagnoli L, Cesareni G | title = Selection of ligands by panning of domain libraries displayed on phage lambda reveals new potential partners of synaptojanin 1 | journal = Journal of Molecular Biology | volume = 307 | issue = 5 | pages = 1329–39 | date = Apr 2001 | pmid = 11292345 | doi = 10.1006/jmbi.2001.4572 }}
* {{vcite2 journal | vauthors = Kimura A, Baumann CA, Chiang SH, Saltiel AR | title = The sorbin homology domain: a motif for the targeting of proteins to lipid rafts | journal = Proceedings of the National Academy of Sciences of the United States of America | volume = 98 | issue = 16 | pages = 9098–103 | date = Jul 2001 | pmid = 11481476 | pmc = 55379 | doi = 10.1073/pnas.151252898 }}
* {{cite journal | vauthors = Kimura A, Baumann CA, Chiang SH, Saltiel AR | title = The sorbin homology domain: a motif for the targeting of proteins to lipid rafts | journal = Proceedings of the National Academy of Sciences of the United States of America | volume = 98 | issue = 16 | pages = 9098–103 | date = Jul 2001 | pmid = 11481476 | pmc = 55379 | doi = 10.1073/pnas.151252898 }}
* {{vcite2 journal | vauthors = Xu YC, Wu RF, Gu Y, Yang YS, Yang MC, Nwariaku FE, Terada LS | title = Involvement of TRAF4 in oxidative activation of c-Jun N-terminal kinase | journal = The Journal of Biological Chemistry | volume = 277 | issue = 31 | pages = 28051–7 | date = Aug 2002 | pmid = 12023963 | doi = 10.1074/jbc.M202665200 }}
* {{cite journal | vauthors = Xu YC, Wu RF, Gu Y, Yang YS, Yang MC, Nwariaku FE, Terada LS | title = Involvement of TRAF4 in oxidative activation of c-Jun N-terminal kinase | journal = The Journal of Biological Chemistry | volume = 277 | issue = 31 | pages = 28051–7 | date = Aug 2002 | pmid = 12023963 | doi = 10.1074/jbc.M202665200 }}
* {{vcite2 journal | vauthors = Nakayama M, Kikuno R, Ohara O | title = Protein-protein interactions between large proteins: two-hybrid screening using a functionally classified library composed of long cDNAs | journal = Genome Research | volume = 12 | issue = 11 | pages = 1773–84 | date = Nov 2002 | pmid = 12421765 | pmc = 187542 | doi = 10.1101/gr.406902 }}
* {{cite journal | vauthors = Nakayama M, Kikuno R, Ohara O | title = Protein-protein interactions between large proteins: two-hybrid screening using a functionally classified library composed of long cDNAs | journal = Genome Research | volume = 12 | issue = 11 | pages = 1773–84 | date = Nov 2002 | pmid = 12421765 | pmc = 187542 | doi = 10.1101/gr.406902 }}
* {{vcite2 journal | vauthors = Soubeyran P, Barac A, Szymkiewicz I, Dikic I | title = Cbl-ArgBP2 complex mediates ubiquitination and degradation of c-Abl | journal = The Biochemical Journal | volume = 370 | issue = Pt 1 | pages = 29–34 | date = Feb 2003 | pmid = 12475393 | pmc = 1223168 | doi = 10.1042/BJ20021539 }}
* {{cite journal | vauthors = Soubeyran P, Barac A, Szymkiewicz I, Dikic I | title = Cbl-ArgBP2 complex mediates ubiquitination and degradation of c-Abl | journal = The Biochemical Journal | volume = 370 | issue = Pt 1 | pages = 29–34 | date = Feb 2003 | pmid = 12475393 | pmc = 1223168 | doi = 10.1042/BJ20021539 }}
* {{vcite2 journal | vauthors = Haglund K, Ivankovic-Dikic I, Shimokawa N, Kruh GD, Dikic I | title = Recruitment of Pyk2 and Cbl to lipid rafts mediates signals important for actin reorganization in growing neurites | journal = Journal of Cell Science | volume = 117 | issue = Pt 12 | pages = 2557–68 | date = May 2004 | pmid = 15128873 | doi = 10.1242/jcs.01148 }}
* {{cite journal | vauthors = Haglund K, Ivankovic-Dikic I, Shimokawa N, Kruh GD, Dikic I | title = Recruitment of Pyk2 and Cbl to lipid rafts mediates signals important for actin reorganization in growing neurites | journal = Journal of Cell Science | volume = 117 | issue = Pt 12 | pages = 2557–68 | date = May 2004 | pmid = 15128873 | doi = 10.1242/jcs.01148 }}
* {{vcite2 journal | vauthors = Beausoleil SA, Jedrychowski M, Schwartz D, Elias JE, Villén J, Li J, Cohn MA, Cantley LC, Gygi SP | title = Large-scale characterization of HeLa cell nuclear phosphoproteins | journal = Proceedings of the National Academy of Sciences of the United States of America | volume = 101 | issue = 33 | pages = 12130–5 | date = Aug 2004 | pmid = 15302935 | pmc = 514446 | doi = 10.1073/pnas.0404720101 }}
* {{cite journal | vauthors = Beausoleil SA, Jedrychowski M, Schwartz D, Elias JE, Villén J, Li J, Cohn MA, Cantley LC, Gygi SP | title = Large-scale characterization of HeLa cell nuclear phosphoproteins | journal = Proceedings of the National Academy of Sciences of the United States of America | volume = 101 | issue = 33 | pages = 12130–5 | date = Aug 2004 | pmid = 15302935 | pmc = 514446 | doi = 10.1073/pnas.0404720101 }}
* {{vcite2 journal | vauthors = Wiemann S, Arlt D, Huber W, Wellenreuther R, Schleeger S, Mehrle A, Bechtel S, Sauermann M, Korf U, Pepperkok R, Sültmann H, Poustka A | title = From ORFeome to biology: a functional genomics pipeline | journal = Genome Research | volume = 14 | issue = 10B | pages = 2136–44 | date = Oct 2004 | pmid = 15489336 | pmc = 528930 | doi = 10.1101/gr.2576704 }}
* {{cite journal | vauthors = Wiemann S, Arlt D, Huber W, Wellenreuther R, Schleeger S, Mehrle A, Bechtel S, Sauermann M, Korf U, Pepperkok R, Sültmann H, Poustka A | title = From ORFeome to biology: a functional genomics pipeline | journal = Genome Research | volume = 14 | issue = 10B | pages = 2136–44 | date = Oct 2004 | pmid = 15489336 | pmc = 528930 | doi = 10.1101/gr.2576704 }}
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Revision as of 09:45, 2 August 2015

Template:PBB ArgBP2 protein, also referred to as Sorbin and SH3 domain-containing protein 2 is a protein that in humans is encoded by the SORBS2 gene.[1][2] ArgBP2 belongs to the a small family of adaptor proteins having sorbin homology (SOHO) domains. ArgBP2 is highly abundant in cardiac muscle cells at sarcomeric Z-disc structures, and is expressed in other cells at actin stress fibers and the nucleus.

Structure

ArgBP2 may exist in as many as 9 unique isoforms ranging from 52 kDa to 117 kDa (492 to 1100 amino acids).[2] ArgBP2 belongs to the a small family of adaptor proteins having sorbin homology (SOHO) domains and three SH3 domains, which regulate cell adhesion, cytoskeletal organization and growth factor signaling; other members include CAP/ponsin and vinexin.[3] The three SH3 domains are C-terminal, a serine-threonine rich domain[4] resides in the middle, and the sorbin homology (SoHo) domain is N-terminal. The SH3 domains interact with Arg/Abl, vinculin.[3] The SOHO domain interacts with flotillin found in lipid rafts.[5]

Function

The subcellular localization of this protein in epithelial and cardiac muscle cells suggests that ArgBP2 functions as an adapter protein to assemble signaling complexes in stress fibers, and that it is a potential link between Abl family kinases and the actin cytoskeleton. ArgBP2 contains several potential Abl phosphorylation sites;[4] Arg and c-Abl represent the mammalian members of the Abelson family of non-receptor protein-tyrosine kinases. In non-muscle cells, ArgBP2 bids Cbl which enhances the degradation of c-Abl;[6] and also Pyk2 which promotes cytoskeletal remodeling.[7] ArgBP2 binding with flotillin at lipid rafts may indicate a role for ArgBP2 in vesicle trafficking and signal transduction. Interestingly, flotillin in skeletal muscle cells exhibits a striated pattern[8] suggesting localization to T-tubules or sarcoplasmic reticular cisternae, though no precise role has been determined in cardiac cells. In cardiac muscle cells, pull-down experiments discovered ArgBP2 in complex with alpha actinin-2, vinculin, spectrin, paxillin, Pyk2 and flotillin, suggesting that ArgBP2 may be involved in myofibril assembly and Z-band signaling in cardiomyocytes,[9] though functional studies are necessary to elucidate specific mechanisms. ArgBP2 has been linked to hyertrophic signaling, as a potent paracrine-acting RNA molecule shown to induce cardiac hypertrophy in mice, miR-21, acts on both ArgBP2 and PDLIM5 to trigger the hypertrophic response.[10]

Clinical Significance

Elevated levels of serum ArgBP2 and coordinate decreases in ArgBP2 in myocardial tissue were detected in the very early phase from patients post-myocardial infarction who died within 7 hours of the insult.[11] Chromosome 4 pericentric inversion has been observed in 10 patients, with associated cardiac defects linked to terminal 4q35.1 deletions, which may affect SORBS2.[12]

Interactions

ArgBP2 has been shown to interact with:

References

  1. ^ a b c Wang B, Golemis EA, Kruh GD (Jul 1997). "ArgBP2, a multiple Src homology 3 domain-containing, Arg/Abl-interacting protein, is phosphorylated in v-Abl-transformed cells and localized in stress fibers and cardiocyte Z-disks". The Journal of Biological Chemistry. 272 (28): 17542–50. doi:10.1074/jbc.272.28.17542. PMID 9211900.{{cite journal}}: CS1 maint: unflagged free DOI (link) Cite error: The named reference "pmid9211900" was defined multiple times with different content (see the help page).
  2. ^ a b "Entrez Gene: SORBS2 sorbin and SH3 domain containing 2".
  3. ^ a b Kioka N, Ueda K, Amachi T (Feb 2002). "Vinexin, CAP/ponsin, ArgBP2: a novel adaptor protein family regulating cytoskeletal organization and signal transduction". Cell Structure and Function. 27 (1): 1–7. PMID 11937713.
  4. ^ a b Wang B, Golemis EA, Kruh GD (Jul 1997). "ArgBP2, a multiple Src homology 3 domain-containing, Arg/Abl-interacting protein, is phosphorylated in v-Abl-transformed cells and localized in stress fibers and cardiocyte Z-disks". The Journal of Biological Chemistry. 272 (28): 17542–50. PMID 9211900.
  5. ^ Kimura A, Baumann CA, Chiang SH, Saltiel AR (Jul 2001). "The sorbin homology domain: a motif for the targeting of proteins to lipid rafts". Proceedings of the National Academy of Sciences of the United States of America. 98 (16): 9098–103. doi:10.1073/pnas.151252898. PMID 11481476.
  6. ^ Soubeyran P, Barac A, Szymkiewicz I, Dikic I (Feb 2003). "Cbl-ArgBP2 complex mediates ubiquitination and degradation of c-Abl". The Biochemical Journal. 370 (Pt 1): 29–34. doi:10.1042/BJ20021539. PMID 12475393.
  7. ^ Haglund K, Ivankovic-Dikic I, Shimokawa N, Kruh GD, Dikic I (May 2004). "Recruitment of Pyk2 and Cbl to lipid rafts mediates signals important for actin reorganization in growing neurites". Journal of Cell Science. 117 (Pt 12): 2557–68. doi:10.1242/jcs.01148. PMID 15128873.
  8. ^ Voldstedlund M, Vinten J, Tranum-Jensen J (Nov 2001). "cav-p60 expression in rat muscle tissues. Distribution of caveolar proteins". Cell and Tissue Research. 306 (2): 265–76. doi:10.1007/s004410100439. PMID 11702238.
  9. ^ a b c Sanger JM, Wang J, Gleason LM, Chowrashi P, Dube DK, Mittal B, Zhukareva V, Sanger JW (Dec 2010). "Arg/Abl-binding protein, a Z-body and Z-band protein, binds sarcomeric, costameric, and signaling molecules". Cytoskeleton. 67 (12): 808–23. doi:10.1002/cm.20490. PMID 20886612.
  10. ^ Bang C, Batkai S, Dangwal S, Gupta SK, Foinquinos A, Holzmann A, Just A, Remke J, Zimmer K, Zeug A, Ponimaskin E, Schmiedl A, Yin X, Mayr M, Halder R, Fischer A, Engelhardt S, Wei Y, Schober A, Fiedler J, Thum T (May 2014). "Cardiac fibroblast-derived microRNA passenger strand-enriched exosomes mediate cardiomyocyte hypertrophy". The Journal of Clinical Investigation. 124 (5): 2136–46. doi:10.1172/JCI70577. PMID 24743145.
  11. ^ Kakimoto Y, Ito S, Abiru H, Kotani H, Ozeki M, Tamaki K, Tsuruyama T. "Sorbin and SH3 domain-containing protein 2 is released from infarcted heart in the very early phase: proteomic analysis of cardiac tissues from patients". Journal of the American Heart Association. 2 (6): e000565. doi:10.1161/JAHA.113.000565. PMID 24342996.
  12. ^ Maurin ML, Labrune P, Brisset S, Le Lorc'h M, Pineau D, Castel C, Romana S, Tachdjian G (Feb 2009). "Molecular cytogenetic characterization of a 4p15.1-pter duplication and a 4q35.1-qter deletion in a recombinant of chromosome 4 pericentric inversion". American Journal of Medical Genetics. Part A. 149A (2): 226–31. doi:10.1002/ajmg.a.32603. PMID 19161154.
  13. ^ a b Soubeyran P, Barac A, Szymkiewicz I, Dikic I (Feb 2003). "Cbl-ArgBP2 complex mediates ubiquitination and degradation of c-Abl". Biochem. J. 370 (Pt 1): 29–34. doi:10.1042/BJ20021539. PMC 1223168. PMID 12475393.
  14. ^ Sanger JM, Wang J, Gleason LM, Chowrashi P, Dube DK, Mittal B, Zhukareva V, Sanger JW (Dec 2010). "Arg/Abl-binding protein, a Z-body and Z-band protein, binds sarcomeric, costameric, and signaling molecules". Cytoskeleton (Hoboken). 67 (12): 808–23. doi:10.1002/cm.20490. PMC 3019100. PMID 20886612.
  15. ^ a b Haglund K, Ivankovic-Dikic I, Shimokawa N, Kruh GD, Dikic I (May 2004). "Recruitment of Pyk2 and Cbl to lipid rafts mediates signals important for actin reorganization in growing neurites". J. Cell. Sci. 117 (Pt 12): 2557–68. doi:10.1242/jcs.01148. PMID 15128873.
  16. ^ Kimura A, Baumann CA, Chiang SH, Saltiel AR (Jul 2001). "The sorbin homology domain: a motif for the targeting of proteins to lipid rafts". Proc. Natl. Acad. Sci. U.S.A. 98 (16): 9098–103. doi:10.1073/pnas.151252898. PMC 55379. PMID 11481476.
  17. ^ Rönty M, Taivainen A, Moza M, Kruh GD, Ehler E, Carpen O (Oct 2005). "Involvement of palladin and alpha-actinin in targeting of the Abl/Arg kinase adaptor ArgBP2 to the actin cytoskeleton". Exp. Cell Res. 310 (1): 88–98. doi:10.1016/j.yexcr.2005.06.026. PMID 16125169.
  18. ^ Kioka N, Ueda K, Amachi T (Feb 2002). "Vinexin, CAP/ponsin, ArgBP2: a novel adaptor protein family regulating cytoskeletal organization and signal transduction". Cell Struct. Funct. 27 (1): 1–7. PMID 11937713.

Further reading

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