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Signal transduction by the α 6 β 4 integrin: distinct β 4 subunit sites mediate recruitment of Shc/Grb2 and association with the cytoskeleton of hemidesmosomes
Author(s) -
Mainiero F.,
Pepe A.,
Wary K.K.,
Spinardi L.,
Mohammadi M.,
Schlessinger J.,
Giancotti F.G.
Publication year - 2000
Publication title -
the embo journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 7.484
H-Index - 392
eISSN - 1460-2075
pISSN - 0261-4189
DOI - 10.1093/emboj/19.20.5585
Subject(s) - biology , hemidesmosome , beta (programming language) , cytoskeleton , microbiology and biotechnology , signal transduction , integrin , protein subunit , alpha (finance) , g alpha subunit , genetics , gene , receptor , cell , computer science , medicine , construct validity , nursing , basement membrane , patient satisfaction , programming language
The EMBO Journal , 14 , 4470–4481, 1995The α6β4 integrin is a major receptor for the basement membrane component laminin 5. Ligation of the α6β4 integrin induces tyrosine phosphorylation of the β4 cyto plasmic domain, followed by recruitement of the adaptor protein Shc and activation of mitogen‐activated protein (MAP) kinase cascades (Mainiero et al ., 1995, 1997). In addition to its signaling function, the cytoplasmic domain of β4 plays a crucial role in the assembly of hemidesmosomes (Spinardi et al ., 1993; Murgia et …