Sqd interacts with the Drosophila retinoblastoma tumor suppressor Rbf.

ABSTRACT: The retinoblastoma tumor suppressor (RB) serves as a scaffold to coordinate binding of numerous proteins, including E2F and histone deacetylases, through its C-terminal domain. The amino-terminal half of RB has few known binding partners and its function is not well understood. We used the amino-terminal domain of the Drosophila retinoblastoma tumor suppressor Rbf (RbfN) to identify novel binding partners by immunoprecipitation coupled with mass spectrometry. Our experiment revealed that the RNA-binding protein Squid (Sqd) is a putative interacting partner of RbfN. Western blot confirmed that Sqd interacts with the amino-terminal domain of Rbf. We observed that Sqd colocalizes with RbfN in Drosophila salivary gland cells. We also show that double RNAi knockdown of Rbf and Sqd in the eye re

SUBMITTER: Ahlander J 

PROVIDER: S-EPMC3926423 | biostudies-literature | 2009 Jun

REPOSITORIES: biostudies-literature