Linked Life Data

10413605

Source:http://linkedlifedata.com/resource/pubmed/id/10413605

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1999-8-19
pubmed:abstractText
Integrins are transmembrane proteins linking the extracellular matrix or certain cell-cell contacts to the cytoskeleton. To study integrin-cytoskeleton interactions we wanted to relate talin-integrin interaction to integrin function in cell spreading and formation of focal adhesions. For talin-binding studies we used fusion proteins of glutathione S-transferase and the cytoplasmic domain of integrin beta(1) (GST-cytobeta(1)) expressed in bacteria. For functional studies chimeric integrins containing the extracellular and transmembrane parts of beta(3) linked to the cytoplasmic domain of beta(1) were expressed in CHO cells as a dimer with the alpha(IIb) subunit. Point mutations in the amino acid sequence N(785)PIY(788) of beta(1) disrupted both the integrin-talin interaction and the ability of the integrin to mediate cell spreading. COOH-terminal truncation of beta(1) at the amino acid position 797 disrupted its ability to mediate cell spreading, whereas the disruption of talin binding required deletion of five more amino acids (truncation at position 792). A synthetic peptide from this region of beta(1) (W(780)DTGENPIYKSAV(792)) bound to purified talin and inhibited talin binding to GST-cytobeta(1). The ability of the mutants to mediate focal adhesion formation or to codistribute to focal adhesions formed by other integrins correlated with their ability to mediate cell spreading. These results confirm the previous finding that a talin-binding site in the integrin beta(1) tail resides at or close to the central NPXY motif and suggest that the integrin-talin interaction is necessary but not sufficient for integrin-mediated cell spreading.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Aug
pubmed:issn
0014-4827
pubmed:author
pubmed:copyrightInfo
Copyright 1999 Academic Press.
pubmed:issnType
Print
pubmed:day
1
pubmed:volume
250
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
524-34
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed-meshheading:10413605-3T3 Cells, pubmed-meshheading:10413605-Amino Acid Sequence, pubmed-meshheading:10413605-Animals, pubmed-meshheading:10413605-Antigens, CD, pubmed-meshheading:10413605-Antigens, CD29, pubmed-meshheading:10413605-Binding Sites, pubmed-meshheading:10413605-CHO Cells, pubmed-meshheading:10413605-Cell Adhesion, pubmed-meshheading:10413605-Cell Size, pubmed-meshheading:10413605-Cricetinae, pubmed-meshheading:10413605-Cytoplasm, pubmed-meshheading:10413605-Fibrinogen, pubmed-meshheading:10413605-Fluorescent Antibody Technique, pubmed-meshheading:10413605-Integrin beta3, pubmed-meshheading:10413605-Mice, pubmed-meshheading:10413605-Molecular Sequence Data, pubmed-meshheading:10413605-Mutation, pubmed-meshheading:10413605-Peptide Fragments, pubmed-meshheading:10413605-Platelet Membrane Glycoproteins, pubmed-meshheading:10413605-Protein Binding, pubmed-meshheading:10413605-Recombinant Fusion Proteins, pubmed-meshheading:10413605-Talin, pubmed-meshheading:10413605-Transfection
pubmed:year
1999
pubmed:articleTitle
Effects of mutations in the cytoplasmic domain of integrin beta(1) to talin binding and cell spreading.
pubmed:affiliation
Division of Biochemistry, University of Helsinki, Helsinki, Finland.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't