التفاصيل البيبلوغرافية
| العنوان: |
Inhibitory Member of the Apoptosis-stimulating Proteins of the p53 Family (iASPP) Interacts with Protein Phosphatase 1 via a Noncanonical Binding Motif. |
| المؤلفون: |
Llanos, Susana1,2, Royer, Christophe1, Lu, Min1, Bergamaschi, Daniele1,3, Lee, Wen Hwa4, Lu, Xin1 xin.lu@ludwig.ox.ac.uk |
| المصدر: |
Journal of Biological Chemistry. 12/16/2011, Vol. 286 Issue 50, p43039-43044. 6p. |
| مصطلحات موضوعية: |
*PHOSPHOPROTEIN phosphatases, *HUMAN genome, *CELL culture, *RENILLA luciferase, *PROTEASE inhibitors, *APOPTOSIS |
| مستخلص: |
Although kinase mutations have been identified in various human diseases, much less is known about protein phosphatases. Here, we show that all apoptosis-stimulating proteins of p53 (ASPP) family members can bind protein phosphatase 1 (PP1) via two distinct interacting motifs. ASPP2 interacts with PP1 through an RVXF PP1 binding motif, whereas the inhibitory member of the ASPP family (iASPP) interacts with PP1 via a noncanonical motif (RNYF) that is located within its Src homology 3 domain (SH3). Phe-815 is crucial in mediating iASPP/PP1 interaction, and iASPP(F815A) fails to inhibit the transcriptional and apoptotic function of p53. This study identifies iASPP as a new binding partner of PP1, interacting through a noncanonical PP1 binding motif. [ABSTRACT FROM AUTHOR] |
| قاعدة البيانات: |
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