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Integrin beta-2 is a protein that in humans is encoded by the ITGB2 gene.
CD18 is the beta subunit of three different structures:
- LFA-1 (paired with CD11a)
- Macrophage-1 antigen (paired with CD11b)
- Integrin alphaXbeta2 (paired with CD11c)
The ITGB2 protein product is the integrin beta chain beta 2. 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. For example, beta 2 combines with the alpha L chain to form the integrin LFA-1, and combines with the alpha M chain to form the integrin Mac-1. Integrins are known to participate in cell adhesion as well as cell-surface mediated signalling.[1]
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Interactions
CD18 has been shown to interact with ICAM-1,[2][3][4] FHL2,[5] PSCD1[6][7] and GNB2L1.[8]
References
- ^ "Entrez Gene: ITGB2 integrin, beta 2 (complement component 3 receptor 3 and 4 subunit)". http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3689.
- ^ Kotovuori, A; Pessa-Morikawa T, Kotovuori P, Nortamo P, Gahmberg C G (Jun. 1999). "ICAM-2 and a peptide from its binding domain are efficient activators of leukocyte adhesion and integrin affinity". J. Immunol. (UNITED STATES) 162 (11): 6613-20. ISSN 0022-1767. PMID 10352278.
- ^ Lu, C; Takagi J, Springer T A (May. 2001). "Association of the membrane proximal regions of the alpha and beta subunit cytoplasmic domains constrains an integrin in the inactive state". J. Biol. Chem. (United States) 276 (18): 14642-8. doi:. ISSN 0021-9258. PMID 11279101.
- ^ Huang, C; Springer T A (Aug. 1995). "A binding interface on the I domain of lymphocyte function-associated antigen-1 (LFA-1) required for specific interaction with intercellular adhesion molecule 1 (ICAM-1)". J. Biol. Chem. (UNITED STATES) 270 (32): 19008-16. ISSN 0021-9258. PMID 7642561.
- ^ 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:. ISSN 0021-9258. PMID 10906324.
- ^ Rietzler, M; Bittner M, Kolanus W, Schuster A, Holzmann B (Oct. 1998). "The human WD repeat protein WAIT-1 specifically interacts with the cytoplasmic tails of beta7-integrins". J. Biol. Chem. (UNITED STATES) 273 (42): 27459-66. ISSN 0021-9258. PMID 9765275.
- ^ Geiger, C; Nagel W, Boehm T, van Kooyk Y, Figdor C G, Kremmer E, Hogg N, Zeitlmann L, Dierks H, Weber K S, Kolanus W (Jun. 2000). "Cytohesin-1 regulates beta-2 integrin-mediated adhesion through both ARF-GEF function and interaction with LFA-1". EMBO J. (ENGLAND) 19 (11): 2525-36. doi:. ISSN 0261-4189. PMID 10835351.
- ^ 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. ISSN 0021-9258. PMID 9442085.
Further reading
- Bunting M, Harris ES, McIntyre TM, et al. (2002). "Leukocyte adhesion deficiency syndromes: adhesion and tethering defects involving beta 2 integrins and selectin ligands.". Curr. Opin. Hematol. 9 (1): 30–5. doi:. PMID 11753075.
- Roos D, Law SK (2003). "Hematologically important mutations: leukocyte adhesion deficiency.". Blood Cells Mol. Dis. 27 (6): 1000–4. doi:. PMID 11831866.
- Gahmberg CG, Fagerholm S (2003). "Activation of leukocyte beta2-integrins.". Vox Sang. 83 Suppl 1: 355–8. PMID 12617168.
- Schymeinsky J, Mócsai A, Walzog B (2007). "Neutrophil activation via beta2 integrins (CD11/CD18): molecular mechanisms and clinical implications.". Thromb. Haemost. 98 (2): 262–73. PMID 17721605.
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