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PMID: 7796809 Published · ppublish English 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.

The LAR transmembrane protein tyrosine phosphatase and a coiled-coil LAR-interacting protein co-localize at focal adhesions.

The EMBO journal ·Vol. 14 ·No. 12 ·1995-06-15 ·Pages 2827-38

Serra-Pagès C, Kedersha NL, Fazikas L, Medley Q, Debant A, Streuli M

Abstract

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.

MeSH Terms
Adaptor Proteins, Signal Transducing Amino Acid Sequence Cell Adhesion/physiology Cloning, Molecular Cytoplasm/metabolism Extracellular Matrix/metabolism Humans 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
Chemicals
Adaptor Proteins, Signal Transducing PPFIA1 protein, human Phosphoproteins RNA, Messenger Receptors, Cell Surface Recombinant Fusion Proteins PTPRA protein, human Protein Tyrosine Phosphatases Receptor-Like Protein Tyrosine Phosphatases, Class 4
Authors & Affiliations
6 authors, click to expand affiliations / ORCID
Serra-Pagès C
Division of Tumor Immunology, Dana-Farber Cancer Institute, Boston, MA 02115, USA.
Kedersha N L
Fazikas L
Medley Q
Debant A
Streuli M
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Article Info
Journal
The EMBO journal
Abbr.
EMBO J
ISSN
0261-4189
Published
1995-06-15
Pages
2827-38
Language
English
Region
England
NLM ID
8208664
PMCID
PMC398401
Subset
IM
Grants
NCI NIH HHS · CA55547 · United States
Databases
GENBANK
U22815, U22816
External Links
PubMed source PMC Full Text View journal details
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