ASPP proteins discriminate between PP1 catalytic subunits through their SH3 domain and the PP1 C-tail

M. Teresa Bertran; Stéphane Mouilleron; Yanxiang Zhou; Rakhi Bajaj; Federico Uliana; Ganesan Senthil Kumar; Audrey van Drogen; Rebecca Lee; Jennifer J. Banerjee; Simon Hauri; Nicola O’Reilly; Matthias Gstaiger; Rebecca Page; Wolfgang Peti; Nicolas Tapon

doi:10.1038/s41467-019-08686-0

Nature Communications (Feb 2019)

ASPP proteins discriminate between PP1 catalytic subunits through their SH3 domain and the PP1 C-tail

M. Teresa Bertran,
Stéphane Mouilleron,
Yanxiang Zhou,
Rakhi Bajaj,
Federico Uliana,
Ganesan Senthil Kumar,
Audrey van Drogen,
Rebecca Lee,
Jennifer J. Banerjee,
Simon Hauri,
Nicola O’Reilly,
Matthias Gstaiger,
Rebecca Page,
Wolfgang Peti,
Nicolas Tapon

Affiliations

M. Teresa Bertran: Apoptosis and Proliferation Control Laboratory, The Francis Crick Institute
Stéphane Mouilleron: Structural Biology - Science Technology Platform, The Francis Crick Institute
Yanxiang Zhou: Apoptosis and Proliferation Control Laboratory, The Francis Crick Institute
Rakhi Bajaj: Chemistry and Biochemistry Department, University of Arizona
Federico Uliana: Department of Biology, Institute of Molecular Systems Biology, ETH Zürich
Ganesan Senthil Kumar: Chemistry and Biochemistry Department, University of Arizona
Audrey van Drogen: Department of Biology, Institute of Molecular Systems Biology, ETH Zürich
Rebecca Lee: Structural Biology - Science Technology Platform, The Francis Crick Institute
Jennifer J. Banerjee: Apoptosis and Proliferation Control Laboratory, The Francis Crick Institute
Simon Hauri: Department of Biology, Institute of Molecular Systems Biology, ETH Zürich
Nicola O’Reilly: Peptide Chemistry Laboratory, The Francis Crick Institute
Matthias Gstaiger: Department of Biology, Institute of Molecular Systems Biology, ETH Zürich
Rebecca Page: Chemistry and Biochemistry Department, University of Arizona
Wolfgang Peti: Chemistry and Biochemistry Department, University of Arizona
Nicolas Tapon: Apoptosis and Proliferation Control Laboratory, The Francis Crick Institute

DOI: https://doi.org/10.1038/s41467-019-08686-0
Journal volume & issue: Vol. 10, no. 1
pp. 1 – 19

Abstract

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Serine/threonine phosphatases such as PP1 associate with a large array of subunit proteins, such as ASPP (apoptosis-stimulating protein of p53) to achieve selective targeting. Here authors solved the crystal structure of the human ASPP2/PP1 complex and explain how ASPP2 can distinguish between PP1 isoforms.

Published in Nature Communications

ISSN: 2041-1723 (Online)
Publisher: Nature Portfolio
Country of publisher: United Kingdom
LCC subjects: Science
Website: https://www.nature.com/ncomms/

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