InterPro : IPR015439

Name  Integrin beta-2 subunit Short Name  Integrin_bsu-2
Type  Family Description  Integrins are the major metazoan receptors for cell adhesion to extracellular matrix proteins and, in vertebrates, also play important roles in certain cell-cell adhesions, make transmembrane connections to the cytoskeleton and activate many intracellular signalling pathways [, ]. The integrin receptors are composed of alpha and beta subunit heterodimers. Each subunit crosses the membraneonce, with most of the polypeptide residing in the extracellular space, and has two short cytoplasmic domains. Some members of this family have EGF repeats at the C terminus and also have a vWA domain inserted within the integrin domain at the N terminus.Most integrins recognise relatively short peptide motifs, and in general require an acidic amino acid to be present. Ligand specificity depends upon both the alpha and beta subunits []. There are at least 18 types of alpha and 8 types of beta subunits recognised in humans []. Each alpha subunit tends to associate only with one type of beta subunit, but there are exceptions to this rule []. Each association of alpha and beta subunits has its own binding specificity and signalling properties. Many integrins require activation on the cell surface before they can bind ligands. Integrins frequently intercommunicate, and binding at one integrin receptor activate or inhibit another.Integrin Beta-2 is also referred to as ITGB2 and is known to interact with three different alpha integrin chains: ITGAL, ITGAM and ITGAX. These three integrin heterodimers are associated with leukocyte adhesion deficiency (LAD), which is characterised by recurrent bacterial infections. LFA-1 (ITGB2/ITGAL) is one of the most well studied of these integrins. Engagement of LFA-1 results in increased AP-1 dependent gene expression, which is mediated by the nuclear translocation of JAB1 []. The ligand for LFA-1 is JAM-1, a member of the endothelial immunoglobulin superfamily. JAM-1 contributes to LFA-1 dependent transendothelial migration of leukocytes and LFA-1 mediated arrest of T cells []. Studies of marginal zone (MZ) B cells also showed that LFA-1, together with alpha4beta1, is required for localisation of those cells in the splenic MZ and that these integrins are necessary for lymphoid tissue compartmentalization [].
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Sequence Features

GO Displayer

Proteins

InterPro protein domain ID --> Contigs

 

Other

0 Child Features

5 Contains

Id Name Short Name Type
IPR002035 von Willebrand factor, type A VWF_A Domain
IPR013111 EGF-like domain, extracellular EGF_extracell Domain
IPR014836 Integrin beta subunit, cytoplasmic domain Integrin_bsu_cyt_dom Domain
IPR002369 Integrin beta subunit, N-terminal Integrin_bsu_N Domain
IPR012896 Integrin beta subunit, tail Integrin_bsu_tail Domain

0 Found In

1 Parent Features

Id Name Short Name Type
IPR015812 Integrin beta subunit Integrin_bsu Family

8 Publications

First Author Title Year Journal Volume Pages
Hynes RO Integrins: bidirectional, allosteric signaling machines. 2002 Cell 110 673-87
Demetriou MC Integrin clipping: a novel adhesion switch? 2004 J Cell Biochem 91 26-35
Cheresh DA A novel vitronectin receptor integrin (alpha v beta x) is responsible for distinct adhesive properties of carcinoma cells. 1989 Cell 57 59-69
Bökel C Integrins in development: moving on, responding to, and sticking to the extracellular matrix. 2002 Dev Cell 3 311-21
Arnaout MA Integrin structure: new twists and turns in dynamic cell adhesion. 2002 Immunol Rev 186 125-40
Bianchi E Integrin LFA-1 interacts with the transcriptional co-activator JAB1 to modulate AP-1 activity. 2000 Nature 404 617-21
Ostermann G JAM-1 is a ligand of the beta(2) integrin LFA-1 involved in transendothelial migration of leukocytes. 2002 Nat Immunol 3 151-8
Lu TT Integrin-mediated long-term B cell retention in the splenic marginal zone. 2002 Science 297 409-12



To cite PlanMine, please refer to the following publication:

Rozanski, A., Moon, H., Brandl, H., Martín-Durán, J. M., Grohme, M., Hüttner, K., Bartscherer, K., Henry, I., & Rink, J. C.
PlanMine 3.0—improvements to a mineable resource of flatworm biology and biodiversity
Nucleic Acids Research, gky1070. doi:10.1093/nar/gky1070 (2018)