Linked Life Data

9614087

Source:http://linkedlifedata.com/resource/pubmed/id/9614087

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
24
pubmed:dateCreated
1998-7-13
pubmed:abstractText
Signal transduction through phosphoinositide 3-OH kinase (PI 3-kinase) has been implicated in the regulation of lymphocyte adhesion mediated by integrin receptors. Cellular phosphorylation products of PI 3-kinases interact with a subset of pleckstrin homology (PH) domains, a module that has been shown to recruit proteins to cellular membranes. We have recently identified cytohesin-1, a cytoplasmic regulator of beta2 integrin adhesion to intercellular adhesion molecule 1. We describe here that expression of a constitutively active PI 3-kinase is sufficient for the activation of Jurkat cell adhesion to intercellular adhesion molecule 1, and for enhanced membrane association of cytohesin-1. Up-regulation of cell adhesion by PI 3-kinase and membrane association of endogenous cytohesin-1 is abrogated by overexpression of the isolated cytohesin-1 PH domain, but not by a mutant of the PH domain which fails to associate with the plasma membrane. The PH domain of Bruton's tyrosine kinase (Btk), although strongly associated with the plasma membrane, had no effect on either membrane recruitment of cytohesin-1 or on induction of adhesion by PI 3-kinase. Having delineated the critical steps of the beta2 integrin activation pathway by biochemical and functional analyses, we conclude that PI 3-kinase activates inside-out signaling of beta2 integrins at least partially through cytohesin-1.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jun
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
12
pubmed:volume
273
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
14853-61
pubmed:dateRevised
2011-11-2
pubmed:meshHeading
pubmed-meshheading:9614087-Antigens, CD18, pubmed-meshheading:9614087-Cell Adhesion, pubmed-meshheading:9614087-Cell Adhesion Molecules, pubmed-meshheading:9614087-Cell Membrane, pubmed-meshheading:9614087-Enzyme Activation, pubmed-meshheading:9614087-Fluorescent Antibody Technique, pubmed-meshheading:9614087-Gene Expression Regulation, Enzymologic, pubmed-meshheading:9614087-Guanine Nucleotide Exchange Factors, pubmed-meshheading:9614087-Humans, pubmed-meshheading:9614087-Immunoglobulin G, pubmed-meshheading:9614087-Intercellular Adhesion Molecule-1, pubmed-meshheading:9614087-Jurkat Cells, pubmed-meshheading:9614087-Phosphatidylinositol 3-Kinases, pubmed-meshheading:9614087-Protein-Tyrosine Kinases, pubmed-meshheading:9614087-Recombinant Fusion Proteins, pubmed-meshheading:9614087-Signal Transduction, pubmed-meshheading:9614087-Up-Regulation
pubmed:year
1998
pubmed:articleTitle
Phosphoinositide 3-OH kinase activates the beta2 integrin adhesion pathway and induces membrane recruitment of cytohesin-1.
pubmed:affiliation
Laboratorium für Molekulare Biologie, Genzentrum der Universität München, Feodor-Lynen-Strasse 25, 81377 München, Germany.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't