Inhibitory Member of the Apoptosis-stimulating Proteins of the p53 Family (iASPP) Interacts with Protein Phosphatase 1 via a Noncanonical Binding Motif

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 P...

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Autores principales: Llanos, Susana, Royer, Christophe, Lu, Min, Bergamaschi, Daniele, Lee, Wen Hwa, Lu, Xin
Formato: Online Artículo Texto
Lenguaje:English
Publicado: American Society for Biochemistry and Molecular Biology 2011
Materias:
Cell Biology
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3234852/
https://www.ncbi.nlm.nih.gov/pubmed/21998301
http://dx.doi.org/10.1074/jbc.M111.270751
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author Llanos, Susana
Royer, Christophe
Lu, Min
Bergamaschi, Daniele
Lee, Wen Hwa
Lu, Xin
author_facet Llanos, Susana
Royer, Christophe
Lu, Min
Bergamaschi, Daniele
Lee, Wen Hwa
Lu, Xin
author_sort Llanos, Susana
collection PubMed
description 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.
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spelling pubmed-32348522011-12-12 Inhibitory Member of the Apoptosis-stimulating Proteins of the p53 Family (iASPP) Interacts with Protein Phosphatase 1 via a Noncanonical Binding Motif Llanos, Susana Royer, Christophe Lu, Min Bergamaschi, Daniele Lee, Wen Hwa Lu, Xin J Biol Chem Cell Biology 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. American Society for Biochemistry and Molecular Biology 2011-12-16 2011-10-13 /pmc/articles/PMC3234852/ /pubmed/21998301 http://dx.doi.org/10.1074/jbc.M111.270751 Text en © 2011 by The American Society for Biochemistry and Molecular Biology, Inc. Author's Choice—Final version full access. Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/3.0/) applies to Author Choice Articles
spellingShingle Cell Biology
Llanos, Susana
Royer, Christophe
Lu, Min
Bergamaschi, Daniele
Lee, Wen Hwa
Lu, Xin
Inhibitory Member of the Apoptosis-stimulating Proteins of the p53 Family (iASPP) Interacts with Protein Phosphatase 1 via a Noncanonical Binding Motif
title Inhibitory Member of the Apoptosis-stimulating Proteins of the p53 Family (iASPP) Interacts with Protein Phosphatase 1 via a Noncanonical Binding Motif
title_full Inhibitory Member of the Apoptosis-stimulating Proteins of the p53 Family (iASPP) Interacts with Protein Phosphatase 1 via a Noncanonical Binding Motif
title_fullStr Inhibitory Member of the Apoptosis-stimulating Proteins of the p53 Family (iASPP) Interacts with Protein Phosphatase 1 via a Noncanonical Binding Motif
title_full_unstemmed Inhibitory Member of the Apoptosis-stimulating Proteins of the p53 Family (iASPP) Interacts with Protein Phosphatase 1 via a Noncanonical Binding Motif
title_short Inhibitory Member of the Apoptosis-stimulating Proteins of the p53 Family (iASPP) Interacts with Protein Phosphatase 1 via a Noncanonical Binding Motif
title_sort inhibitory member of the apoptosis-stimulating proteins of the p53 family (iaspp) interacts with protein phosphatase 1 via a noncanonical binding motif
topic Cell Biology
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3234852/
https://www.ncbi.nlm.nih.gov/pubmed/21998301
http://dx.doi.org/10.1074/jbc.M111.270751
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