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Journal article

Inhibitory member of the apoptosis-stimulating proteins of the p53 family (iASPP) interacts with protein phosphatase 1 via a noncanonical binding motif.

Abstract:

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 (S...

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Publication status:
Published

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Publisher copy:
10.1074/jbc.m111.270751

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Institution:
University of Oxford
Department:
Oxford, MSD, Physiology Anatomy and Genetics
Bergamaschi, D More by this author
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Journal:
The Journal of biological chemistry
Volume:
286
Issue:
50
Pages:
43039-43044
Publication date:
2011-12-05
DOI:
EISSN:
1083-351X
ISSN:
0021-9258
URN:
uuid:de965f21-2469-457d-a6bf-10fdcf7011a0
Source identifiers:
221400
Local pid:
pubs:221400

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