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The paxillin LD motifs
Author(s) -
Tumbarello David A,
Brown Michael C,
Turner Christopher E
Publication year - 2002
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(01)03244-6
Subject(s) - paxillin , signal transducing adaptor protein , microbiology and biotechnology , ptk2 , focal adhesion , cell adhesion , biology , actin cytoskeleton , integrin , signal transduction , cytoskeleton , actin , cell , genetics , mitogen activated protein kinase kinase , protein kinase c
Adapter/scaffold proteins, through their multidomain structure, perform a fundamental role in facilitating signal transduction within cells. Paxillin is a focal adhesion adapter protein implicated in growth factor‐ as well as integrin‐mediated signaling pathways. The amino‐terminus of paxillin contains five leucine‐rich sequences termed LD motifs. These paxillin LD motifs are highly conserved between species as well as within the paxillin superfamily. They mediate interactions with several structural and regulatory proteins important for coordinating changes in the actin cytoskeleton associated with cell motility and cell adhesion as well as in the regulation of gene expression.