Unknown

Dataset Information

0

SH2-containing inositol 5'-phosphatase inhibits transformation of Abelson murine leukemia virus.


ABSTRACT: v-Abl protein tyrosine kinase encoded by Abelson murine leukemia virus (Ab-MLV) transforms pre-B cells. Transformation requires the phosphatidylinositol 3-kinase (PI3K) pathway. This pathway is antagonized by SH2-containing inositol 5'-phosphatase (SHIP), raising the possibility that v-Abl modulates PI3K signaling through SHIP. Consistent with this, we show that v-Abl expression reduces levels of full-length p145 SHIP in a v-Abl kinase activity-dependent fashion. This event requires signals from the Abl SH2 domain but not the carboxyl terminus. Forced expression of full-length SHIP significantly reduces Ab-MLV pre-B-cell transformation. Therefore, reduction of SHIP protein by v-Abl is a critical component in Ab-MLV transformation.

SUBMITTER: Fessler SP 

PROVIDER: S-EPMC3165847 | biostudies-other | 2011 Sep

REPOSITORIES: biostudies-other

altmetric image

Publications

SH2-containing inositol 5'-phosphatase inhibits transformation of Abelson murine leukemia virus.

Fessler Shawn P SP   Rosenberg Naomi N   Baughn Linda B LB  

Journal of virology 20110622 17


v-Abl protein tyrosine kinase encoded by Abelson murine leukemia virus (Ab-MLV) transforms pre-B cells. Transformation requires the phosphatidylinositol 3-kinase (PI3K) pathway. This pathway is antagonized by SH2-containing inositol 5'-phosphatase (SHIP), raising the possibility that v-Abl modulates PI3K signaling through SHIP. Consistent with this, we show that v-Abl expression reduces levels of full-length p145 SHIP in a v-Abl kinase activity-dependent fashion. This event requires signals from  ...[more]

Similar Datasets

| S-EPMC4226566 | biostudies-literature
| S-EPMC4628863 | biostudies-literature
| S-EPMC3269644 | biostudies-literature
| S-EPMC3533387 | biostudies-literature
| S-EPMC5008355 | biostudies-literature
| S-EPMC3850669 | biostudies-literature
| S-EPMC5446635 | biostudies-literature
| S-EPMC4757810 | biostudies-literature
| S-EPMC10496198 | biostudies-literature
| S-EPMC521861 | biostudies-literature