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PMID: 1725602 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S.

Fibronectin/integrin interaction induces tyrosine phosphorylation of a 120-kDa protein.

Cell regulation ·Vol. 2 ·No. 11 ·1991-11-00 ·Pages 951-64

Guan JL, Trevithick JE, Hynes RO

Abstract

We describe a 120-kDa protein (pp120) that is phosphorylated on tyrosine in cells attached to fibronectin-coated surfaces. The protein appears to be located in focal contacts where it codistributes with beta 1 integrins. pp120 is distinct from the beta 1 subunit of integrins and from vinculin and alpha-actinin. pp120 is rapidly dephosphorylated in cells suspended by trypsinization but becomes rapidly phosphorylated in cells attaching and spreading on fibronectin. Attachment of cells to RGD-containing peptides, polylysine, or concanavalin A is not sufficient to induce phosphorylation of pp120. The 120-kDa cell-binding domain of fibronectin can induce some phosphorylation of pp120, but further phosphorylation occurs in the presence also of the heparin-binding domain of fibronectin. Phosphorylation of pp120 precedes, but is correlated with, subsequent cell spreading. Phosphorylation of pp120 can also be triggered by attachment of cells to anti-integrin antibodies, and this requires the cytoplasmic domain of the integrin beta 1 subunit. Thus interaction of beta 1 integrins with extracellular ligands (fibronectin or antibodies) triggers phosphorylation of an intracellular 120-kDa protein, pp120, that may be involved in the responses of cells to attachment.

MeSH Terms
3T3 Cells Animals Cell Adhesion Fibronectins/metabolism Fluorescent Antibody Technique Integrins/metabolism Mice Molecular Weight Peptide Fragments/metabolism Phosphoproteins/chemistry,metabolism Phosphorylation Phosphotyrosine Protein Binding Signal Transduction Time Factors Tyrosine/analogs & derivatives,metabolism
Chemicals
Fibronectins Integrins Peptide Fragments Phosphoproteins Phosphotyrosine Tyrosine
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Guan J L
Department of Biology, Massachusetts Institute of Technology, Cambridge 02139.
Trevithick J E
Hynes R O
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Article Info
Journal
Cell regulation
Abbr.
Cell Regul
ISSN
1044-2030
DOI
10.1091/mbc.2.11.951
Published
1991-11-00
Pages
951-64
Language
English
Region
United States
NLM ID
9005331
PMCID
PMC361893
Subset
IM
Grants
NCI NIH HHS · P01CA26712 · United States
NCI NIH HHS · R01CA17007 · United States
Corrections
CommentIn
PMID: 22848063
External Links
PubMed source DOI: 10.1091/mbc.2.11.951 PMC Full Text
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