Premium
Integrins: alternative splicing as a mechanism to regulate ligand binding and integrin signaling events
Author(s) -
de Melker Annemieke A.,
Sonnenberg Arnoud
Publication year - 1999
Publication title -
bioessays
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.175
H-Index - 184
eISSN - 1521-1878
pISSN - 0265-9247
DOI - 10.1002/(sici)1521-1878(199906)21:6<499::aid-bies6>3.0.co;2-d
Subject(s) - integrin , alternative splicing , microbiology and biotechnology , biology , rna splicing , extracellular , integrin, beta 6 , splice , signal transduction , cell adhesion , transmembrane protein , cytoplasm , cell adhesion molecule , transmembrane domain , cell , gene , receptor , genetics , messenger rna , rna
Integrins are a family of transmembrane proteins composed of heterodimers of α and β subunits. With their extracellular domain they bind extracellular matrix proteins or other cell surface molecules, and their cytoplasmic domain binds to cytoskeletal and signaling proteins. Thus, they are in an ideal position to transfer information from the extracellular environment to the interior of the cell and vice versa. For several integrin subunits, alternative splicing of mRNA leads to variations in the sequence of both extracellular and cytoplasmic domains. Many integrin splice variants have specific expression patterns, but for some time, functional differences between these variants were not evident. Recent experiments using transfected cell lines and gene targeting of specific splice variants have contributed significantly to our understanding of the function of these splice variants. The results indicate that alternative splicing is a mechanism to subtly regulate the ligand binding and signaling activity of integrins. Bio Essays 21:499–509, 1999. © 1999 John Wiley & Sons, Inc.