Document Detail

The LAR transmembrane protein tyrosine phosphatase and a coiled-coil LAR-interacting protein co-localize at focal adhesions.
MedLine Citation:
PMID:  7796809     Owner:  NLM     Status:  MEDLINE    
Focal adhesions are sites of cell-extracellular matrix interactions that function in anchoring stress fibers to the plasma membrane and in adhesion-mediated signal transduction. Both focal adhesion structure and signaling ability involve protein tyrosine phosphorylation. LAR is a broadly expressed transmembrane protein tyrosine phosphatase comprised of a cell adhesion-like ectodomain and two intracellular protein tyrosine phosphatase domains. We have identified a novel cytoplasmic 160 kDa phosphoserine protein termed LAR-interacting protein 1 (LIP.1), which binds to the LAR membrane-distal D2 protein tyrosine phosphatase domain and appears to localize LAR to focal adhesions. Both LAR and LIP.1 decorate the ends of focal adhesions most proximal to the cell nucleus and are excluded from the distal ends of focal adhesions, thus localizing to regions of focal adhesions presumably undergoing disassembly. We propose that LAR and LIP.1 may regulate the disassembly of focal adhesions and thus help orchestrate cell-matrix interactions.
C Serra-Pagès; N L Kedersha; L Fazikas; Q Medley; A Debant; M Streuli
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, Non-P.H.S.; Research Support, U.S. Gov't, P.H.S.    
Journal Detail:
Title:  The EMBO journal     Volume:  14     ISSN:  0261-4189     ISO Abbreviation:  EMBO J.     Publication Date:  1995 Jun 
Date Detail:
Created Date:  1995-08-03     Completed Date:  1995-08-03     Revised Date:  2009-11-18    
Medline Journal Info:
Nlm Unique ID:  8208664     Medline TA:  EMBO J     Country:  ENGLAND    
Other Details:
Languages:  eng     Pagination:  2827-38     Citation Subset:  IM    
Division of Tumor Immunology, Dana-Farber Cancer Institute, Boston, MA 02115, USA.
Data Bank Information
Bank Name/Acc. No.:
GENBANK/U22815;  U22816
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MeSH Terms
Adaptor Proteins, Signal Transducing
Amino Acid Sequence
Cell Adhesion / physiology*
Cloning, Molecular
Cytoplasm / metabolism
Extracellular Matrix / metabolism
Molecular Sequence Data
Molecular Weight
Organ Specificity
Phosphoproteins / chemistry,  genetics,  metabolism*
Protein Conformation
Protein Structure, Secondary
Protein Tyrosine Phosphatases / metabolism*
RNA, Messenger / analysis
Receptor-Like Protein Tyrosine Phosphatases, Class 4
Receptors, Cell Surface*
Recombinant Fusion Proteins / biosynthesis,  metabolism
Sequence Analysis, DNA
Grant Support
Reg. No./Substance:
0/Adaptor Proteins, Signal Transducing; 0/PPFIA1 protein, human; 0/Phosphoproteins; 0/RNA, Messenger; 0/Receptors, Cell Surface; 0/Recombinant Fusion Proteins; EC protein, human; EC Tyrosine Phosphatases; EC Protein Tyrosine Phosphatases, Class 4

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