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CD49d

 
Wikipedia: CD49d
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Integrin, alpha 4 (antigen CD49D, alpha 4 subunit of VLA-4 receptor)
Identifiers
Symbols ITGA4; CD49D; IA4; MGC90518
External IDs OMIM192975 MGI96603 HomoloGene37364
RNA expression pattern
PBB GE ITGA4 213416 at tn.png
PBB GE ITGA4 205884 at tn.png
PBB GE ITGA4 205885 s at tn.png
More reference expression data
Orthologs
Species Human Mouse
Entrez 3676 16401
Ensembl ENSG00000115232 ENSMUSG00000027009
UniProt P13612 Q78E20
RefSeq NM_000885 (mRNA) NM_010576 (mRNA)
NP_000876 (protein) NP_034706 (protein)
Location Chr 2:
182.03 - 182.11 Mb
Chr 2:
79.06 - 79.13 Mb
PubMed search [1] [2]

CD49d is an integrin alpha subunit. It makes up half of the α4β1 lymphocyte homing receptor.

The product of this gene belongs to the integrin alpha chain family of proteins. Integrins are heterodimeric integral membrane proteins composed of an alpha chain and a beta chain. This gene encodes an alpha 4 chain. Unlike other integrin alpha chains, alpha 4 neither contains an I-domain, nor undergoes disulfide-linked cleavage. Alpha 4 chain associates with either beta 1 chain or beta 7 chain.[1]

Contents

Interactions

CD49d has been shown to interact with LGALS8[2] and Paxillin.[3][4]

References

  1. ^ "Entrez Gene: ITGA4 integrin, alpha 4 (antigen CD49D, alpha 4 subunit of VLA-4 receptor)". http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3676. 
  2. ^ 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. 
  3. ^ Han, J; Liu S, Rose D M, Schlaepfer D D, McDonald H, Ginsberg M H (Nov. 2001). "Phosphorylation of the integrin alpha 4 cytoplasmic domain regulates paxillin binding". J. Biol. Chem. (United States) 276 (44): 40903–9. doi:10.1074/jbc.M102665200. ISSN 0021-9258. PMID 11533025. 
  4. ^ Liu, Shouchun; Kiosses William B, Rose David M, Slepak Marina, Salgia Ravi, Griffin James D, Turner Christopher E, Schwartz Martin A, Ginsberg Mark H (Jun. 2002). "A fragment of paxillin binds the alpha 4 integrin cytoplasmic domain (tail) and selectively inhibits alpha 4-mediated cell migration". J. Biol. Chem. (United States) 277 (23): 20887–94. doi:10.1074/jbc.M110928200. ISSN 0021-9258. PMID 11919182. 

Further reading

  • Humphries MJ, Sheridan J, Mould AP, Newham P (1995). "Mechanisms of VCAM-1 and fibronectin binding to integrin alpha 4 beta 1: implications for integrin function and rational drug design.". Ciba Found. Symp. 189: 177–91; discussion 191–9. PMID 7587632. 
  • Oostendorp RA, Dörmer P (1997). "VLA-4-mediated interactions between normal human hematopoietic progenitors and stromal cells.". Leuk. Lymphoma 24 (5-6): 423–35. PMID 9086434. 
  • Porter JC, Hogg N (1999). "Integrins take partners: cross-talk between integrins and other membrane receptors.". Trends Cell Biol. 8 (10): 390–6. PMID 9789327. 
  • Rose DM, Han J, Ginsberg MH (2003). "Alpha4 integrins and the immune response.". Immunol. Rev. 186: 118–24. PMID 12234367. 
  • O'Connor P (2007). "Natalizumab and the role of alpha 4-integrin antagonism in the treatment of multiple sclerosis.". Expert opinion on biological therapy 7 (1): 123–36. doi:10.1517/14712598.7.1.123. PMID 17150024. 
  • Chan BM, Elices MJ, Murphy E, Hemler ME (1992). "Adhesion to vascular cell adhesion molecule 1 and fibronectin. Comparison of alpha 4 beta 1 (VLA-4) and alpha 4 beta 7 on the human B cell line JY.". J. Biol. Chem. 267 (12): 8366–70. PMID 1373725. 
  • Fernández-Ruiz E, Pardo-Manuel de Villena F, Rubio MA, et al. (1992). "Mapping of the human VLA-alpha 4 gene to chromosome 2q31-q32.". Eur. J. Immunol. 22 (2): 587–90. PMID 1537388. 
  • Rubio M, Nueda A, Vara A, Corbí Lopez AL (1992). "A single mRNA encodes the alpha 150 and alpha 80/70 forms of the alpha subunit of VLA4.". Eur. J. Immunol. 22 (4): 1099–102. PMID 1551405. 
  • Sonnenberg A, Linders CJ, Modderman PW, et al. (1990). "Integrin recognition of different cell-binding fragments of laminin (P1, E3, E8) and evidence that alpha 6 beta 1 but not alpha 6 beta 4 functions as a major receptor for fragment E8.". J. Cell Biol. 110 (6): 2145–55. PMID 1693624. 
  • Teixidó J, Parker CM, Kassner PD, Hemler ME (1992). "Functional and structural analysis of VLA-4 integrin alpha 4 subunit cleavage.". J. Biol. Chem. 267 (3): 1786–91. PMID 1730718. 
  • Rosemblatt M, Vuillet-Gaugler MH, Leroy C, Coulombel L (1991). "Coexpression of two fibronectin receptors, VLA-4 and VLA-5, by immature human erythroblastic precursor cells.". J. Clin. Invest. 87 (1): 6–11. PMID 1824634. 
  • Rosen GD, Birkenmeier TM, Dean DC (1991). "Characterization of the alpha 4 integrin gene promoter.". Proc. Natl. Acad. Sci. U.S.A. 88 (10): 4094–8. PMID 2034655. 
  • Takada Y, Elices MJ, Crouse C, Hemler ME (1989). "The primary structure of the alpha 4 subunit of VLA-4: homology to other integrins and a possible cell-cell adhesion function.". EMBO J. 8 (5): 1361–8. PMID 2788572. 
  • Takada Y, Strominger JL, Hemler ME (1987). "The very late antigen family of heterodimers is part of a superfamily of molecules involved in adhesion and embryogenesis.". Proc. Natl. Acad. Sci. U.S.A. 84 (10): 3239–43. PMID 3033641. 
  • Hemler ME, Huang C, Schwarz L (1987). "The VLA protein family. Characterization of five distinct cell surface heterodimers each with a common 130,000 molecular weight beta subunit.". J. Biol. Chem. 262 (7): 3300–9. PMID 3546305. 
  • Gailit J, Pierschbacher M, Clark RA (1993). "Expression of functional alpha 4 beta 1 integrin by human dermal fibroblasts.". J. Invest. Dermatol. 100 (3): 323–8. PMID 8440915. 
  • Pujades C, Teixidó J, Bazzoni G, Hemler ME (1996). "Integrin alpha 4 cysteines 278 and 717 modulate VLA-4 ligand binding and also contribute to alpha 4/180 formation.". Biochem. J. 313 ( Pt 3): 899–908. PMID 8611173. 
  • Szabo M, McIntyre BW (1996). "Identification of two variants of the human integrin alpha 4 subunit.". Mol. Immunol. 32 (17-18): 1453–4. PMID 8643114. 
  • Mannion BA, Berditchevski F, Kraeft SK, et al. (1996). "Transmembrane-4 superfamily proteins CD81 (TAPA-1), CD82, CD63, and CD53 specifically associated with integrin alpha 4 beta 1 (CD49d/CD29).". J. Immunol. 157 (5): 2039–47. PMID 8757325. 

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