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PMID: 11911889 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S. Review

The paxillin LD motifs.

FEBS letters ·Vol. 513 ·No. 1 ·2002-02-20 ·Pages 114-8

Tumbarello DA, Brown MC, Turner CE

Abstract

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.

MeSH Terms
Amino Acid Sequence Animals Binding Sites Cell Adhesion Molecules/chemistry,metabolism Cytoskeletal Proteins/chemistry,metabolism Humans Molecular Sequence Data Paxillin Phosphoproteins/chemistry,metabolism Protein Structure, Secondary Sequence Alignment Sequence Homology, Amino Acid
Chemicals
Cell Adhesion Molecules Cytoskeletal Proteins PXN protein, human Paxillin Phosphoproteins
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Tumbarello David A
Department of Cell and Developmental Biology, SUNY Upstate Medical University, 750 East Adams Street, Syracuse, NY 13210, USA.
Brown Michael C
Turner Christopher E
Article Info
Journal
FEBS letters
Abbr.
FEBS Lett
ISSN
0014-5793
Published
2002-02-20
Pages
114-8
Language
English
Region
England
NLM ID
0155157
Subset
IM
Grants
NIGMS NIH HHS · R01 GM047607 · United States
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