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Interaction of integrin α 6 β 4 with ErbB3 and implication in heregulin‐induced ErbB3/ErbB2‐mediated DNA synthesis
Author(s) -
Kawano Satoshi,
Mizutani Kiyohito,
Miyata Muneaki,
Ikeda Wataru,
Takai Yoshimi
Publication year - 2010
Publication title -
genes to cells
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.912
H-Index - 115
eISSN - 1365-2443
pISSN - 1356-9597
DOI - 10.1111/j.1365-2443.2010.01438.x
Subject(s) - hemidesmosome , biology , integrin , microbiology and biotechnology , laminin , erbb3 , extracellular matrix , integrin, beta 6 , cell adhesion , cd49c , motility , cell , signal transduction , biochemistry , basement membrane , receptor tyrosine kinase
Integrin α 6 β 4 is abundantly expressed in normal epithelial cells and forms hemidesmosomes, one of cell–extracellular matrix junctions. In many types of cancer cells, integrin α 6 β 4 is up‐regulated, laminin, an integrin α 6 β 4 ‐binding extracellular matrix protein, is cleaved, and hemidesmosomes are disrupted, eventually causing an enhancement of cancer cell movement and a facilitation of their invasion. It was previously shown that integrin α 6 β 4 interacts with ErbB1 and ErbB2 and enhances cell proliferation and motility. Here we show that integrin α 6 β 4 interacts with ErbB3 but not with ErbB1, ErbB2 or ErbB4, and enhances the heregulin‐induced, ErbB3/ErbB2 heterodimer‐mediated DNA synthesis, but not cell motility, in A549 cells.