Document Detail


The paxillin LD motifs.
MedLine Citation:
PMID:  11911889     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
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.
Authors:
David A Tumbarello; Michael C Brown; Christopher E Turner
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, P.H.S.; Review    
Journal Detail:
Title:  FEBS letters     Volume:  513     ISSN:  0014-5793     ISO Abbreviation:  FEBS Lett.     Publication Date:  2002 Feb 
Date Detail:
Created Date:  2002-03-25     Completed Date:  2002-05-07     Revised Date:  2006-11-15    
Medline Journal Info:
Nlm Unique ID:  0155157     Medline TA:  FEBS Lett     Country:  Netherlands    
Other Details:
Languages:  eng     Pagination:  114-8     Citation Subset:  IM    
Affiliation:
Department of Cell and Developmental Biology, SUNY Upstate Medical University, 750 East Adams Street, Syracuse, NY 13210, USA.
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MeSH Terms
Descriptor/Qualifier:
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
Chemical
Reg. No./Substance:
0/Cell Adhesion Molecules; 0/Cytoskeletal Proteins; 0/PXN protein, human; 0/Paxillin; 0/Phosphoproteins

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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