The corepressor mSin3a interacts with the proline-rich domain of p53 and protects p53 from proteasome-mediated degradation.

Volume: 21, Issue: 12, Pages: 3974 - 3985
Published: Jun 15, 2001
Abstract
While the transactivation function of the tumor suppressor p53 is well understood, less is known about the transrepression functions of this protein. We have previously shown that p53 interacts with the corepressor protein mSin3a (hereafter designated Sin3) in vivo and that this interaction is critical for the ability of p53 to repress gene expression. In the present study, we demonstrate that expression of Sin3 results in posttranslational...
Paper Details
Title
The corepressor mSin3a interacts with the proline-rich domain of p53 and protects p53 from proteasome-mediated degradation.
Published Date
Jun 15, 2001
Volume
21
Issue
12
Pages
3974 - 3985
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