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 language | English (US) |
|---|---|
| Pages (from-to) | 23452-23457 |
| Number of pages | 6 |
| Journal | Journal of Biological Chemistry |
| Volume | 271 |
| Issue number | 38 |
| DOIs | |
| State | Published - 1996 |
| Externally published | Yes |
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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 journal › Article
}
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.
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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 -