Platelet-derived growth factor-induced formation of tensin and phosphoinositide 3-kinase complexes

Kurt R. Auger, Zhou Songyang, Su Hao Lo, Thomas M. Roberts, Lan Bo Chen

Research output: Contribution to journalArticle

44 Citations (Scopus)

Abstract

Tensin is an SH2 domain-containing cytoskeletal protein that binds to and caps actin filaments. Investigation of signal transduction mechanisms associated with tensin revealed the presence of phosphoinositide 3-kinase (PI 3-kinase) activity in tensin immunoprecipitates from platelet-derived growth factor-treated cells. Association of PI 3-kinase activity with tensin was transitory, and the amount of activity was approximately 1% of the total PI 3-kinase activity found in anti-phosphotyrosine (anti-pY) immunoprecipitates. In vitro, PI 3-kinase activity associated with the SH2 domain of tensin in a platelet-derived growth factor-dependent manner. The optimal phosphopeptide binding specificity of the SH2 domain of tensin was determined to be phospho- Y (E or D), N, (I, V, or F). Synthetic phosphopeptides containing the sequence YENI could specifically block the association of PI 3-kinase activity with tensin in a dose-dependent manner. These results suggest that PI 3-kinase interacts with the cytoskeleton via the SH2 domain of tensin and may play an important role in platelet-derived growth factor-induced cytoskeletal reorganization that is concomitant with cell migration and proliferation.

Original languageEnglish (US)
Pages (from-to)23452-23457
Number of pages6
JournalJournal of Biological Chemistry
Volume271
Issue number38
DOIs
StatePublished - 1996
Externally publishedYes

Fingerprint

1-Phosphatidylinositol 4-Kinase
Platelet-Derived Growth Factor
Phosphatidylinositols
Phosphotransferases
src Homology Domains
Phosphopeptides
Signal transduction
Phosphotyrosine
Cytoskeletal Proteins
Tensins
Actins
Cytoskeleton
Actin Cytoskeleton
Cells
Association reactions
Cell Movement
Signal Transduction
Cell Proliferation

ASJC Scopus subject areas

  • Biochemistry

Cite this

Platelet-derived growth factor-induced formation of tensin and phosphoinositide 3-kinase complexes. / Auger, Kurt R.; Songyang, Zhou; Lo, Su Hao; Roberts, Thomas M.; Chen, Lan Bo.

In: Journal of Biological Chemistry, Vol. 271, No. 38, 1996, p. 23452-23457.

Research output: Contribution to journalArticle

Auger, Kurt R. ; Songyang, Zhou ; Lo, Su Hao ; Roberts, Thomas M. ; Chen, Lan Bo. / Platelet-derived growth factor-induced formation of tensin and phosphoinositide 3-kinase complexes. In: Journal of Biological Chemistry. 1996 ; Vol. 271, No. 38. pp. 23452-23457.
@article{7156f2adfac9461fb5cd97eb536b327a,
title = "Platelet-derived growth factor-induced formation of tensin and phosphoinositide 3-kinase complexes",
abstract = "Tensin is an SH2 domain-containing cytoskeletal protein that binds to and caps actin filaments. Investigation of signal transduction mechanisms associated with tensin revealed the presence of phosphoinositide 3-kinase (PI 3-kinase) activity in tensin immunoprecipitates from platelet-derived growth factor-treated cells. Association of PI 3-kinase activity with tensin was transitory, and the amount of activity was approximately 1{\%} of the total PI 3-kinase activity found in anti-phosphotyrosine (anti-pY) immunoprecipitates. In vitro, PI 3-kinase activity associated with the SH2 domain of tensin in a platelet-derived growth factor-dependent manner. The optimal phosphopeptide binding specificity of the SH2 domain of tensin was determined to be phospho- Y (E or D), N, (I, V, or F). Synthetic phosphopeptides containing the sequence YENI could specifically block the association of PI 3-kinase activity with tensin in a dose-dependent manner. These results suggest that PI 3-kinase interacts with the cytoskeleton via the SH2 domain of tensin and may play an important role in platelet-derived growth factor-induced cytoskeletal reorganization that is concomitant with cell migration and proliferation.",
author = "Auger, {Kurt R.} and Zhou Songyang and Lo, {Su Hao} and Roberts, {Thomas M.} and Chen, {Lan Bo}",
year = "1996",
doi = "10.1074/jbc.271.38.23452",
language = "English (US)",
volume = "271",
pages = "23452--23457",
journal = "Journal of Biological Chemistry",
issn = "0021-9258",
publisher = "American Society for Biochemistry and Molecular Biology Inc.",
number = "38",

}

TY - JOUR

T1 - Platelet-derived growth factor-induced formation of tensin and phosphoinositide 3-kinase complexes

AU - Auger, Kurt R.

AU - Songyang, Zhou

AU - Lo, Su Hao

AU - Roberts, Thomas M.

AU - Chen, Lan Bo

PY - 1996

Y1 - 1996

N2 - Tensin is an SH2 domain-containing cytoskeletal protein that binds to and caps actin filaments. Investigation of signal transduction mechanisms associated with tensin revealed the presence of phosphoinositide 3-kinase (PI 3-kinase) activity in tensin immunoprecipitates from platelet-derived growth factor-treated cells. Association of PI 3-kinase activity with tensin was transitory, and the amount of activity was approximately 1% of the total PI 3-kinase activity found in anti-phosphotyrosine (anti-pY) immunoprecipitates. In vitro, PI 3-kinase activity associated with the SH2 domain of tensin in a platelet-derived growth factor-dependent manner. The optimal phosphopeptide binding specificity of the SH2 domain of tensin was determined to be phospho- Y (E or D), N, (I, V, or F). Synthetic phosphopeptides containing the sequence YENI could specifically block the association of PI 3-kinase activity with tensin in a dose-dependent manner. These results suggest that PI 3-kinase interacts with the cytoskeleton via the SH2 domain of tensin and may play an important role in platelet-derived growth factor-induced cytoskeletal reorganization that is concomitant with cell migration and proliferation.

AB - Tensin is an SH2 domain-containing cytoskeletal protein that binds to and caps actin filaments. Investigation of signal transduction mechanisms associated with tensin revealed the presence of phosphoinositide 3-kinase (PI 3-kinase) activity in tensin immunoprecipitates from platelet-derived growth factor-treated cells. Association of PI 3-kinase activity with tensin was transitory, and the amount of activity was approximately 1% of the total PI 3-kinase activity found in anti-phosphotyrosine (anti-pY) immunoprecipitates. In vitro, PI 3-kinase activity associated with the SH2 domain of tensin in a platelet-derived growth factor-dependent manner. The optimal phosphopeptide binding specificity of the SH2 domain of tensin was determined to be phospho- Y (E or D), N, (I, V, or F). Synthetic phosphopeptides containing the sequence YENI could specifically block the association of PI 3-kinase activity with tensin in a dose-dependent manner. These results suggest that PI 3-kinase interacts with the cytoskeleton via the SH2 domain of tensin and may play an important role in platelet-derived growth factor-induced cytoskeletal reorganization that is concomitant with cell migration and proliferation.

UR - http://www.scopus.com/inward/record.url?scp=0029833286&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0029833286&partnerID=8YFLogxK

U2 - 10.1074/jbc.271.38.23452

DO - 10.1074/jbc.271.38.23452

M3 - Article

C2 - 8798552

AN - SCOPUS:0029833286

VL - 271

SP - 23452

EP - 23457

JO - Journal of Biological Chemistry

JF - Journal of Biological Chemistry

SN - 0021-9258

IS - 38

ER -