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Integrin beta 3

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(Redirected from CD61)

ITGB3
Available structures
PDBOrtholog search: PDBe RCSB
Identifiers
AliasesITGB3, BDPLT16, BDPLT2, CD61, GP3A, GPIIIa, GT, integrin subunit beta 3, BDPLT24, GT2
External IDsOMIM: 173470; MGI: 96612; HomoloGene: 55444; GeneCards: ITGB3; OMA:ITGB3 - orthologs
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

NM_000212

NM_016780

RefSeq (protein)

NP_000203

NP_058060

Location (UCSC)Chr 17: 47.25 – 47.31 MbChr 11: 104.5 – 104.56 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Integrin beta-3 (β3) or CD61 is a protein that in humans is encoded by the ITGB3 gene.[5] CD61 is a cluster of differentiation found on thrombocytes.[6]

Structure and function

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The ITGB3 protein product is the integrin beta chain beta 3. Integrins are integral cell-surface proteins composed of an alpha chain and a beta chain. A given chain may combine with multiple partners resulting in different integrins. Integrin beta 3 is found along with the alpha IIb chain in platelets. Integrins are known to participate in cell adhesion as well as cell-surface-mediated signaling.[7]

Role in endometriosis

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Defectively expressed β3 integrin subunit has been correlated with presence of endometriosis, and has been suggested as a putative marker of this condition.[8]

Interactions

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CD61 has been shown to interact with PTK2,[9][10] ITGB3BP,[11][12] TLN1[13][14] and CIB1.[15]

See also

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References

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  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000259207Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000020689Ensembl, 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. ^ Sosnoski DM, Emanuel BS, Hawkins AL, van Tuinen P, Ledbetter DH, Nussbaum RL, et al. (June 1988). "Chromosomal localization of the genes for the vitronectin and fibronectin receptors alpha subunits and for platelet glycoproteins IIb and IIIa". The Journal of Clinical Investigation. 81 (6): 1993–1998. doi:10.1172/JCI113548. PMC 442653. PMID 2454952.
  6. ^ Heemskerk JW, Mattheij NJ, Cosemans JM (January 2013). "Platelet-based coagulation: different populations, different functions". Journal of Thrombosis and Haemostasis. 11 (1): 2–16. doi:10.1111/jth.12045. PMID 23106920. S2CID 206157070.
  7. ^ "Entrez Gene: ITGB3 integrin, beta 3 (platelet glycoprotein IIIa, antigen CD61)".
  8. ^ May KE, Villar J, Kirtley S, Kennedy SH, Becker CM (2011). "Endometrial alterations in endometriosis: a systematic review of putative biomarkers". Human Reproduction Update. 17 (5): 637–653. doi:10.1093/humupd/dmr013. PMID 21672902.
  9. ^ Eliceiri BP, Puente XS, Hood JD, Stupack DG, Schlaepfer DD, Huang XZ, et al. (April 2002). "Src-mediated coupling of focal adhesion kinase to integrin alpha(v)beta5 in vascular endothelial growth factor signaling". The Journal of Cell Biology. 157 (1): 149–160. doi:10.1083/jcb.200109079. PMC 2173263. PMID 11927607.
  10. ^ Chung J, Gao AG, Frazier WA (June 1997). "Thrombspondin acts via integrin-associated protein to activate the platelet integrin alphaIIbbeta3". The Journal of Biological Chemistry. 272 (23): 14740–14746. doi:10.1074/jbc.272.23.14740. PMID 9169439.
  11. ^ Fujimoto TT, Katsutani S, Shimomura T, Fujimura K (January 2002). "Novel alternatively spliced form of beta(3)-endonexin". Thrombosis Research. 105 (1): 63–70. doi:10.1016/S0049-3848(01)00405-4. PMID 11864709.
  12. ^ Shattil SJ, O'Toole T, Eigenthaler M, Thon V, Williams M, Babior BM, et al. (November 1995). "Beta 3-endonexin, a novel polypeptide that interacts specifically with the cytoplasmic tail of the integrin beta 3 subunit". The Journal of Cell Biology. 131 (3): 807–816. doi:10.1083/jcb.131.3.807. PMC 2120613. PMID 7593198.
  13. ^ Patil S, Jedsadayanmata A, Wencel-Drake JD, Wang W, Knezevic I, Lam SC (October 1999). "Identification of a talin-binding site in the integrin beta(3) subunit distinct from the NPLY regulatory motif of post-ligand binding functions. The talin n-terminal head domain interacts with the membrane-proximal region of the beta(3) cytoplasmic tail". The Journal of Biological Chemistry. 274 (40): 28575–28583. doi:10.1074/jbc.274.40.28575. PMID 10497223.
  14. ^ Calderwood DA, Yan B, de Pereda JM, Alvarez BG, Fujioka Y, Liddington RC, et al. (June 2002). "The phosphotyrosine binding-like domain of talin activates integrins". The Journal of Biological Chemistry. 277 (24): 21749–21758. doi:10.1074/jbc.M111996200. PMID 11932255.
  15. ^ Naik UP, Patel PM, Parise LV (February 1997). "Identification of a novel calcium-binding protein that interacts with the integrin alphaIIb cytoplasmic domain". The Journal of Biological Chemistry. 272 (8): 4651–4654. doi:10.1074/jbc.272.8.4651. PMID 9030514.

Further reading

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