Linked Life Data

7592789

Source:http://linkedlifedata.com/resource/pubmed/id/7592789

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
43
pubmed:dateCreated
1995-12-14
pubmed:abstractText
Recently we reported the localization of phosphoinositide 3-kinase (PI 3-kinase) by immunofluorescence to microtubule bundles and the centrosome (Kapeller, R., Chakrabarti, R., Cantley, L., Fay, F., and Corvera, S. (1993) Mol. Cell. Biol. 13, 6052-6063). In complementary experiments we used the recombinant p85 subunit of PI 3-kinase to identify proteins that associate with phosphoinositide 3-kinase and found that phosphoinositide 3-kinase associates with alpha/beta-tubulin. The association occurs in vivo but was not significantly affected by growth factor stimulation. We localized the region of p85 that interacts with alpha/beta-tubulin to the inter-SH2 domain. These results support the immunofluorescence data and show that p85 directly associates with alpha/beta-tubulin. We then determined whether phosphoinositide 3-kinase associates with gamma-tubulin. We found a dramatic growth factor-dependent association of phosphoinositide 3-kinase with gamma-tubulin. Phosphoinositide 3-kinase associates with gamma-tubulin in response to insulin and, to a lesser extent, in response to platelet-derived growth factor. Neither epidermal growth factor nor nerve growth factor treatment of cells results in association of phosphoinositide 3-kinase and gamma-tubulin. Phosphoinositide 3-kinase is also immunoprecipitated with antibodies to pericentrin in response to insulin, indicating that phosphoinositide 3-kinase is recruited to the centrosome. Neither phosphoinositide 3-kinase activity, nor intact microtubules are necessary for the association. Treatment of cells with 0.5 M NaCl dissociates gamma-tubulin from the centrosome and disrupts the association of phosphoinositide 3-kinase with pericentrin, but not gamma-tubulin. Recombinant p85 binds to gamma-tubulin from both insulin stimulated and quiescent cells. These results suggest that the association of phosphoinositide 3-kinase with gamma-tubulin is direct. These data suggest that phosphoinositide 3-kinase may be involved in regulating microtubule responses to insulin and platelet-derived growth factor.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Oct
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
27
pubmed:volume
270
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
25985-91
pubmed:dateRevised
2011-11-17
pubmed:meshHeading
pubmed-meshheading:7592789-3T3 Cells, pubmed-meshheading:7592789-Amino Acid Sequence, pubmed-meshheading:7592789-Animals, pubmed-meshheading:7592789-Antigens, pubmed-meshheading:7592789-Binding Sites, pubmed-meshheading:7592789-Blotting, Western, pubmed-meshheading:7592789-CHO Cells, pubmed-meshheading:7592789-Centrosome, pubmed-meshheading:7592789-Cricetinae, pubmed-meshheading:7592789-Insulin, pubmed-meshheading:7592789-Mice, pubmed-meshheading:7592789-Microtubule-Associated Proteins, pubmed-meshheading:7592789-Molecular Sequence Data, pubmed-meshheading:7592789-PC12 Cells, pubmed-meshheading:7592789-Phosphatidylinositol 3-Kinases, pubmed-meshheading:7592789-Phosphotransferases (Alcohol Group Acceptor), pubmed-meshheading:7592789-Platelet-Derived Growth Factor, pubmed-meshheading:7592789-Precipitin Tests, pubmed-meshheading:7592789-Protein Binding, pubmed-meshheading:7592789-Rats, pubmed-meshheading:7592789-Recombinant Fusion Proteins, pubmed-meshheading:7592789-Tubulin
pubmed:year
1995
pubmed:articleTitle
Phosphoinositide 3-kinase binds constitutively to alpha/beta-tubulin and binds to gamma-tubulin in response to insulin.
pubmed:affiliation
Department of Medicine, Beth Israel Hospital, Boston, Massachusetts 02215, USA.
pubmed:publicationType
Journal Article, Comparative Study, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't