Integrin beta-1 is a protein that in humans is encoded by the ITGB1 gene.[1] CD29 is an integrin unit associated with very late antigen receptors. It is known to conjoin with alpha-3 subunit to create α3β1 complex that reacts to such molecules as netrin-1 and reelin.
Integrins are heterodimeric proteins made up of alpha and beta subunits. At least 18 alpha and 8 beta subunits have been described in mammals. Integrin family members are membrane receptors involved in cell adhesion and recognition in a variety of processes including embryogenesis, hemostasis, tissue repair, immune response and metastatic diffusion of tumor cells. The protein encoded by this gene is a beta subunit. Six alternatively spliced variants have been found for this gene which encode five proteins with alternate carboxy termini.[2]
[edit] Interactions
CD29 has been shown to interact with TSPAN4,[3] CD9,[4][5] Filamin,[6][7] FLNB,[6] CD81,[5][8] CD46,[9] MAP4K4,[10] FHL2,[11] NME1,[12] PKC alpha,[13][14] YWHAB,[15] ITGB1BP1,[16][17] LGALS8[18] and GNB2L1.[13][19] A neutralizing antibody for CD29 is AIIB2.
[edit] References
- ^ Goodfellow PJ, Nevanlinna HA, Gorman P, Sheer D, Lam G, Goodfellow PN (Jul 1989). "Assignment of the gene encoding the beta-subunit of the human fibronectin receptor (beta-FNR) to chromosome 10p11.2". Ann Hum Genet 53 (Pt 1): 15–22. doi:10.1111/j.1469-1809.1989.tb01118.x. PMID 2524991.
- ^ "Entrez Gene: ITGB1 integrin, beta 1 (fibronectin receptor, beta polypeptide, antigen CD29 includes MDF2, MSK12)". http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3688.
- ^ Tachibana, I; Bodorova J, Berditchevski F, Zutter M M, Hemler M E (Nov. 1997). "NAG-2, a novel transmembrane-4 superfamily (TM4SF) protein that complexes with integrins and other TM4SF proteins". J. Biol. Chem. (UNITED STATES) 272 (46): 29181–9. doi:10.1074/jbc.272.46.29181. ISSN 0021-9258. PMID 9360996.
- ^ Radford, K J; Thorne R F, Hersey P (May. 1996). "CD63 associates with transmembrane 4 superfamily members, CD9 and CD81, and with beta 1 integrins in human melanoma". Biochem. Biophys. Res. Commun. (UNITED STATES) 222 (1): 13–8. doi:10.1006/bbrc.1996.0690. ISSN 0006-291X. PMID 8630057.
- ^ a b Mazzocca, Antonio; Carloni Vinicio, Sciammetta Silvia, Cordella Claudia, Pantaleo Pietro, Caldini Anna, Gentilini Paolo, Pinzani Massimo (Sep. 2002). "Expression of transmembrane 4 superfamily (TM4SF) proteins and their role in hepatic stellate cell motility and wound healing migration". J. Hepatol. (England) 37 (3): 322–30. doi:10.1016/S0168-8278(02)00175-7. ISSN 0168-8278. PMID 12175627.
- ^ a b van der Flier, Arjan; Kuikman Ingrid, Kramer Duco, Geerts Dirk, Kreft Maaike, Takafuta Toshiro, Shapiro Sandor S, Sonnenberg Arnoud (Jan. 2002). "Different splice variants of filamin-B affect myogenesis, subcellular distribution, and determine binding to integrin β subunits". J. Cell Biol. (United States) 156 (2): 361–76. doi:10.1083/jcb.200103037. ISSN 0021-9525. PMC 2199218. PMID 11807098. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=2199218.
- ^ Loo, D T; Kanner S B, Aruffo A (Sep. 1998). "Filamin binds to the cytoplasmic domain of the beta1-integrin. Identification of amino acids responsible for this interaction". J. Biol. Chem. (UNITED STATES) 273 (36): 23304–12. doi:10.1074/jbc.273.36.23304. ISSN 0021-9258. PMID 9722563.
- ^ Serru, V; Le Naour F, Billard M, Azorsa D O, Lanza F, Boucheix C, Rubinstein E (May. 1999). "Selective tetraspan-integrin complexes (CD81/alpha4beta1, CD151/alpha3beta1, CD151/alpha6beta1) under conditions disrupting tetraspan interactions". Biochem. J. (ENGLAND) 340 (Pt 1): 103–11. doi:10.1042/0264-6021:3400103. ISSN 0264-6021. PMC 1220227. PMID 10229664. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1220227.
- ^ Lozahic, S; Christiansen D, Manié S, Gerlier D, Billard M, Boucheix C, Rubinstein E (Mar. 2000). "CD46 (membrane cofactor protein) associates with multiple beta1 integrins and tetraspans". Eur. J. Immunol. (GERMANY) 30 (3): 900–7. doi:10.1002/1521-4141(200003)30:3<900::AID-IMMU900>3.0.CO;2-X. ISSN 0014-2980. PMID 10741407.
- ^ Poinat, Patrice; De Arcangelis Adèle, Sookhareea Satis, Zhu Xiaoping, Hedgecock Edward M, Labouesse Michel, Georges-Labouesse Elisabeth (Apr. 2002). "A conserved interaction between beta1 integrin/PAT-3 and Nck-interacting kinase/MIG-15 that mediates commissural axon navigation in C. elegans". Curr. Biol. (England) 12 (8): 622–31. doi:10.1016/S0960-9822(02)00764-9. ISSN 0960-9822. PMID 11967148.
- ^ Wixler, V; Geerts D, Laplantine E, Westhoff D, Smyth N, Aumailley M, Sonnenberg A, Paulsson M (Oct. 2000). "The LIM-only protein DRAL/FHL2 binds to the cytoplasmic domain of several alpha and beta integrin chains and is recruited to adhesion complexes". J. Biol. Chem. (UNITED STATES) 275 (43): 33669–78. doi:10.1074/jbc.M002519200. ISSN 0021-9258. PMID 10906324.
- ^ Fournier, Henri-Noël; Dupé-Manet Sandra, Bouvard Daniel, Lacombe Marie-Lise, Marie Christiane, Block Marc R, Albiges-Rizo Corinne (Jun. 2002). "Integrin cytoplasmic domain-associated protein 1alpha (ICAP-1alpha ) interacts directly with the metastasis suppressor nm23-H2, and both proteins are targeted to newly formed cell adhesion sites upon integrin engagement". J. Biol. Chem. (United States) 277 (23): 20895–902. doi:10.1074/jbc.M200200200. ISSN 0021-9258. PMID 11919189.
- ^ a b Lee, H-S; Millward-Sadler S J, Wright M O, Nuki G, Al-Jamal R, Salter D M (Nov. 2002). "Activation of Integrin-RACK1/PKCalpha signalling in human articular chondrocyte mechanotransduction". Osteoarthr. Cartil. (England) 10 (11): 890–7. doi:10.1053/joca.2002.0842. ISSN 1063-4584. PMID 12435334.
- ^ Parsons, Maddy; Keppler Melanie D, Kline Adam, Messent Anthea, Humphries Martin J, Gilchrist Ruth, Hart Ian R, Quittau-Prevostel Corinne, Hughes William E, Parker Peter J, Ng Tony (Aug. 2002). "Site-Directed Perturbation of Protein Kinase C- Integrin Interaction Blocks Carcinoma Cell Chemotaxis". Mol. Cell. Biol. (United States) 22 (16): 5897–911. doi:10.1128/MCB.22.16.5897-5911.2002. ISSN 0270-7306. PMC 133968. PMID 12138200. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=133968.
- ^ Han, D C; Rodriguez L G, Guan J L (Jan. 2001). "Identification of a novel interaction between integrin beta1 and 14-3-3beta". Oncogene (England) 20 (3): 346–57. doi:10.1038/sj.onc.1204068. ISSN 0950-9232. PMID 11313964.
- ^ Chang, D D; Wong C, Smith H, Liu J (Sep. 1997). "ICAP-1, a Novel β1 Integrin Cytoplasmic Domain–associated Protein, Binds to a Conserved and Functionally Important NPXY Sequence Motif of β1 Integrin". J. Cell Biol. (UNITED STATES) 138 (5): 1149–57. doi:10.1083/jcb.138.5.1149. ISSN 0021-9525. PMC 2136751. PMID 9281591. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=2136751.
- ^ Chang, David D; Hoang Bao Q, Liu Jenny, Springer Timothy A (Mar. 2002). "Molecular basis for interaction between Icap1 alpha PTB domain and beta 1 integrin". J. Biol. Chem. (United States) 277 (10): 8140–5. doi:10.1074/jbc.M109031200. ISSN 0021-9258. PMID 11741908.
- ^ Hadari, Y R; Arbel-Goren R, Levy Y, Amsterdam A, Alon R, Zakut R, Zick Y (Jul. 2000). "Galectin-8 binding to integrins inhibits cell adhesion and induces apoptosis". J. Cell. Sci. (ENGLAND) 113 ( Pt 13): 2385–97. ISSN 0021-9533. PMID 10852818.
- ^ Liliental, J; Chang D D (Jan. 1998). "Rack1, a receptor for activated protein kinase C, interacts with integrin beta subunit". J. Biol. Chem. (UNITED STATES) 273 (4): 2379–83. doi:10.1074/jbc.273.4.2379. ISSN 0021-9258. PMID 9442085.
[edit] Further reading
- Evans JP (2001). "Fertilin beta and other ADAMs as integrin ligands: insights into cell adhesion and fertilization". Bioessays 23 (7): 628–39. doi:10.1002/bies.1088. PMID 11462216.
- Armulik A (2002). "Splice variants of human beta 1 integrins: origin, biosynthesis and functions". Front. Biosci. 7: d219–27. doi:10.2741/armulik. PMID 11779688.
- Brakebusch C, Fässler R (2006). "beta 1 integrin function in vivo: adhesion, migration and more". Cancer Metastasis Rev. 24 (3): 403–11. doi:10.1007/s10555-005-5132-5. PMID 16258728.
[edit] External links
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CD1 ( a-c, 1A, 1D, 1E) · CD2 · CD3 ( γ, δ, ε) · CD4 · CD5 · CD6 · CD7 · CD8 ( a) · CD9 · CD10 · CD11 ( a, b, c) · CD13 · CD14 · CD15 · CD16 ( A, B) · CD18 · CD19 · CD20 · CD21 · CD22 · CD23 · CD24 · CD25 · CD26 · CD27 · CD28 · CD29 · CD30 · CD31 · CD32 ( A, B) · CD33 · CD34 · CD35 · CD36 · CD37 · CD38 · CD39 · CD40 · CD41 · CD42 ( a, b, c, d) · CD43 · CD44 · CD45 · CD46 · CD47 · CD48 · CD49 ( a, b, c, d, e, f) · CD50
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CD51 · CD52 · CD53 · CD54 · CD55 · CD56 · CD57 · CD58 · CD59 · CD61 · CD62 ( E, L, P) · CD63 · CD64 ( A, B, C) · CD66 ( a, b, c, d, e, f) · CD68 · CD69 · CD70 · CD71 · CD72 · CD73 · CD74 · CD78 · CD79 ( a, b) · CD80 · CD81 · CD82 · CD83 · CD84 · CD85 ( a, d, e, h, j, k) · CD86 · CD87 · CD88 · CD89 · CD90 · CD91- CD92 · CD93 · CD94 · CD95 · CD96 · CD97 · CD98 · CD99 · CD100
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CD151 · CD152 · CD153 · CD154 · CD155 · CD156 ( a, b, c) · CD157 · CD158 ( a, d, e, i, k) · CD159 ( a, c) · CD160 · CD161 · CD162 · CD163 · CD164 · CD166 · CD167 ( a, b) · CD168 · CD169 · CD170 · CD171 · CD172 ( a, b, g) · CD174 · CD177 · CD178 · CD179 ( a, b) · CD181 · CD182 · CD183 · CD184 · CD185 · CD186 · CD191 · CD192 · CD193 · CD194 · CD195 · CD196 · CD197 · CDw198 · CDw199 · CD200
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see also cell surface receptor deficiencies
B trdu: iter (nrpl/grfl/cytl/horl), csrc (lgic, enzr, gprc, igsr, intg, nrpr/grfr/cytr), itra (adap, gbpr, mapk), calc, lipd; path (hedp, wntp, tgfp+mapp, notp, jakp, fsap, hipp, tlrp)
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