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GIPC1

From Wikipedia, the free encyclopedia
GIPC1
Identifiers
AliasesGIPC1, C19orf3, GIPC, GLUT1CBP, Hs.6454, IIP-1, NIP, RGS19IP1, SEMCAP, SYNECTIIN, SYNECTIN, TIP-2, GIPC PDZ domain containing family member 1, OPDM2
External IDsOMIM: 605072; MGI: 1926252; HomoloGene: 21167; GeneCards: GIPC1; OMA:GIPC1 - orthologs
Orthologs
SpeciesHumanMouse
Entrez

10755

67903

Ensembl

ENSG00000123159

ENSMUSG00000019433

UniProt

O14908

Q9Z0G0

RefSeq (mRNA)

NM_018771

RefSeq (protein)

NP_005707
NP_974197
NP_974198
NP_974199
NP_974223

NP_061241

Location (UCSC)Chr 19: 14.48 – 14.5 MbChr 8: 84.38 – 84.39 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

GIPC PDZ domain containing family, member 1 (GIPC1) is a protein that in humans is encoded by the GIPC1 gene.[5][6][7] GIPC was originally identified as it binds specifically to the C terminus of RGS-GAIP, a protein involved in the regulation of G protein signaling.[5] GIPC is an acronym for "GAIP Interacting Protein C-terminus". RGS proteins are "Regulators of G protein Signaling" and RGS-GAIP is a "GTPase Activator protein for Gαi/Gαq", which are two major subtypes of Gα proteins. The human GIPC1 molecule is 333 amino acids or about 36 kDa in molecular size and consists of a central PDZ domain, a compact protein module which mediates specific protein-protein interactions. The RGS-GAIP protein interacts with this domain and many other proteins interact here or at other parts of the GIPC1 molecule. As a result, GIPC1 was independently discovered by several other groups and has a variety of alternate names, including synectin, C19orf3, RGS19IP1 and others. The GIPC1 gene family in mammals consisting of three members, so the first discovered, originally named GIPC, is now generally called GIPC1, with the other two being named GIPC2 and GIPC3.[8] The three human proteins are about 60% identical in protein sequence. GIPC1 has been shown to interact with a variety of other receptor and cytoskeletal proteins including the GLUT1 receptor, ACTN1, KIF1B, MYO6, PLEKHG5, SDC4/syndecan-4, SEMA4C/semaphorin-4 and HTLV-I Tax. The general function of GIPC family proteins therefore appears to be mediating specific interactions between proteins involved in G protein signaling and membrane translocation.

Interactions

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GIPC1 has been shown to interact with:

See also

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GIPC PDZ domain containing family, member 2, GIPC2

GIPC PDZ domain containing family, member 3, GIPC3

References

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  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000123159 – Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000019433 – Ensembl, May 2017
  3. ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. ^ a b De Vries L, Lou X, Zhao G, Zheng B, Farquhar MG (November 1998). "GIPC, a PDZ domain containing protein, interacts specifically with the C terminus of RGS-GAIP". Proc. Natl. Acad. Sci. U.S.A. 95 (21): 12340–5. Bibcode:1998PNAS...9512340D. doi:10.1073/pnas.95.21.12340. PMC 22833. PMID 9770488.
  6. ^ Rousset R, Fabre S, Desbois C, Bantignies F, Jalinot P (March 1998). "The C-terminus of the HTLV-1 Tax oncoprotein mediates interaction with the PDZ domain of cellular proteins". Oncogene. 16 (5): 643–54. doi:10.1038/sj.onc.1201567. PMID 9482110.
  7. ^ "Entrez Gene: GIPC1 GIPC PDZ domain containing family, member 1".
  8. ^ Katoh M (2002). "GIPC gene family (Review)". Int. J. Mol. Med. 9 (6): 585–9. doi:10.3892/ijmm.9.6.585. PMID 12011974.
  9. ^ a b c Bunn RC, Jensen MA, Reed BC (April 1999). "Protein interactions with the glucose transporter binding protein GLUT1CBP that provide a link between GLUT1 and the cytoskeleton". Mol. Biol. Cell. 10 (4): 819–32. doi:10.1091/mbc.10.4.819. PMC 25204. PMID 10198040.
  10. ^ Hu LA, Chen W, Martin NP, Whalen EJ, Premont RT, Lefkowitz RJ (July 2003). "GIPC interacts with the beta1-adrenergic receptor and regulates beta1-adrenergic receptor-mediated ERK activation". J. Biol. Chem. 278 (28): 26295–301. doi:10.1074/jbc.M212352200. PMID 12724327.
  11. ^ a b Tani TT, Mercurio AM (September 2001). "PDZ interaction sites in integrin alpha subunits. T14853, TIP/GIPC binds to a type I recognition sequence in alpha 6A/alpha 5 and a novel sequence in alpha 6B". J. Biol. Chem. 276 (39): 36535–42. doi:10.1074/jbc.M105785200. PMID 11479315.
  12. ^ a b Gotthardt M, Trommsdorff M, Nevitt MF, Shelton J, Richardson JA, Stockinger W, Nimpf J, Herz J (August 2000). "Interactions of the low density lipoprotein receptor gene family with cytosolic adaptor and scaffold proteins suggest diverse biological functions in cellular communication and signal transduction". J. Biol. Chem. 275 (33): 25616–24. doi:10.1074/jbc.M000955200. PMID 10827173.
  13. ^ Petersen HH, Hilpert J, Militz D, Zandler V, Jacobsen C, Roebroek AJ, Willnow TE (February 2003). "Functional interaction of megalin with the megalinbinding protein (MegBP), a novel tetratrico peptide repeat-containing adaptor molecule". J. Cell Sci. 116 (Pt 3): 453–61. doi:10.1242/jcs.00243. PMID 12508107.
  14. ^ Lou X, McQuistan T, Orlando RA, Farquhar MG (April 2002). "GAIP, GIPC and Galphai3 are concentrated in endocytic compartments of proximal tubule cells: putative role in regulating megalin's function". J. Am. Soc. Nephrol. 13 (4): 918–27. doi:10.1681/ASN.V134918. PMID 11912251.
  15. ^ Hirakawa T, Galet C, Kishi M, Ascoli M (December 2003). "GIPC binds to the human lutropin receptor (hLHR) through an unusual PDZ domain binding motif, and it regulates the sorting of the internalized human choriogonadotropin and the density of cell surface hLHR". J. Biol. Chem. 278 (49): 49348–57. doi:10.1074/jbc.M306557200. PMID 14507927.
  16. ^ Ewing RM, Chu P, Elisma F, Li H, Taylor P, Climie S, McBroom-Cerajewski L, Robinson MD, O'Connor L, Li M, Taylor R, Dharsee M, Ho Y, Heilbut A, Moore L, Zhang S, Ornatsky O, Bukhman YV, Ethier M, Sheng Y, Vasilescu J, Abu-Farha M, Lambert JP, Duewel HS, Stewart II, Kuehl B, Hogue K, Colwill K, Gladwish K, Muskat B, Kinach R, Adams SL, Moran MF, Morin GB, Topaloglou T, Figeys D (2007). "Large-scale mapping of human protein-protein interactions by mass spectrometry". Mol. Syst. Biol. 3: 89. doi:10.1038/msb4100134. PMC 1847948. PMID 17353931.
  17. ^ Aschenbrenner L, Lee T, Hasson T (July 2003). "Myo6 facilitates the translocation of endocytic vesicles from cell peripheries". Mol. Biol. Cell. 14 (7): 2728–43. doi:10.1091/mbc.E02-11-0767. PMC 165672. PMID 12857860.
  18. ^ Lou X, Yano H, Lee F, Chao MV, Farquhar MG (March 2001). "GIPC and GAIP form a complex with TrkA: a putative link between G protein and receptor tyrosine kinase pathways". Mol. Biol. Cell. 12 (3): 615–27. doi:10.1091/mbc.12.3.615. PMC 30968. PMID 11251075.
  19. ^ Awan A, Lucic MR, Shaw DM, Sheppard F, Westwater C, Lyons SA, Stern PL (January 2002). "5T4 interacts with TIP-2/GIPC, a PDZ protein, with implications for metastasis". Biochem. Biophys. Res. Commun. 290 (3): 1030–6. doi:10.1006/bbrc.2001.6288. PMID 11798178.
  20. ^ Liu TF, Kandala G, Setaluri V (September 2001). "PDZ domain protein GIPC interacts with the cytoplasmic tail of melanosomal membrane protein gp75 (tyrosinase-related protein-1)". J. Biol. Chem. 276 (38): 35768–77. doi:10.1074/jbc.M103585200. PMID 11441007.

Further reading

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