Integrin cytoplasmic interactions and bidirectional transmembrane signalling
- PMID: 8939656
- DOI: 10.1016/s0955-0674(96)80107-4
Integrin cytoplasmic interactions and bidirectional transmembrane signalling
Abstract
Integrins are heterodimeric integral plasma membrane proteins containing extracellular, transmembrane, and cytoplasmic domains. These highly versatile receptors mediate not only cell adhesion and migration, but also the bidirectional transfer of information across the plasma membrane. The cytoplasmic domains of integrins are required for the transduction of this bidirectional information, and have recently been shown to participate in direct interactions with some novel cytoplasmic proteins, such as an ankyrin repeat containing serine/threonine protein kinase (integrin-linked kinase) and beta3 endonexin. New evidence also suggests that, via interactions with focal adhesion kinase, the integrin cytoplasmic domains can coordinate actin cytoskeletal organization and responses to growth factors. The elucidation of the signal transduction pathways activated by integrins is an intense area of investigation that has shown that integrins have some unique properties as signal transducing receptors.
Similar articles
-
Integrins in cell adhesion and signaling.Hum Cell. 1996 Sep;9(3):181-6. Hum Cell. 1996. PMID: 9183647 Review.
-
alpha1 Integrin cytoplasmic domain is involved in focal adhesion formation via association with intracellular proteins.Biochem J. 2001 May 15;356(Pt 1):233-40. doi: 10.1042/0264-6021:3560233. Biochem J. 2001. PMID: 11336656 Free PMC article.
-
Integrins interact with focal adhesions through multiple distinct pathways.J Cell Physiol. 1999 Oct;181(1):74-82. doi: 10.1002/(SICI)1097-4652(199910)181:1<74::AID-JCP8>3.0.CO;2-H. J Cell Physiol. 1999. PMID: 10457355
-
Focal adhesion kinase and paxillin bind to peptides mimicking beta integrin cytoplasmic domains.J Cell Biol. 1995 Sep;130(5):1181-7. doi: 10.1083/jcb.130.5.1181. J Cell Biol. 1995. PMID: 7657702 Free PMC article.
-
Integrin cytoplasmic domains as connectors to the cell's signal transduction apparatus.Matrix Biol. 1997 Oct;16(4):153-63. doi: 10.1016/s0945-053x(97)90003-2. Matrix Biol. 1997. PMID: 9402004 Review.
Cited by
-
The roles of two distinct regions of PINCH-1 in the regulation of cell attachment and spreading.Mol Biol Cell. 2010 Dec;21(23):4120-9. doi: 10.1091/mbc.E10-05-0459. Epub 2010 Oct 6. Mol Biol Cell. 2010. PMID: 20926685 Free PMC article.
-
Aluminum-induced gene expression and protein localization of a cell wall-associated receptor kinase in Arabidopsis.Plant Physiol. 2003 Aug;132(4):2256-66. doi: 10.1104/pp.103.022129. Plant Physiol. 2003. PMID: 12913180 Free PMC article.
-
Concerted action of two avirulent spore effectors activates Reaction to Puccinia graminis 1 (Rpg1)-mediated cereal stem rust resistance.Proc Natl Acad Sci U S A. 2011 Aug 30;108(35):14676-81. doi: 10.1073/pnas.1111771108. Epub 2011 Aug 22. Proc Natl Acad Sci U S A. 2011. PMID: 21873196 Free PMC article.
-
Fibronectin: functional character and role in alcoholic liver disease.World J Gastroenterol. 2011 May 28;17(20):2482-99. doi: 10.3748/wjg.v17.i20.2482. World J Gastroenterol. 2011. PMID: 21633653 Free PMC article. Review.
-
Transmembrane-truncated alphavbeta3 integrin retains high affinity for ligand binding: evidence for an 'inside-out' suppressor?Biochem J. 1998 Mar 1;330 ( Pt 2)(Pt 2):861-9. doi: 10.1042/bj3300861. Biochem J. 1998. PMID: 9480902 Free PMC article.
Publication types
MeSH terms
Substances
LinkOut - more resources
Full Text Sources
Other Literature Sources