Proteomics

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Kawashima_Phosphorylation_PHLPP1_2020_TripleTOF6600

ABSTRACT: This dataset consists of 20 raw MS files and associated peak lists and result files, acquired on AB SCIEX 6600 TripleTOF mass spectrometer operated in Data Dependent Acquisition mode. Samples were generated by Cassandra Wong. Affinity purifications, mass spectrometry acquisition and analysis were also performed by Cassandra Wong under the supervision Anne-Claude Gingras. The files are associated with a manuscript submitted for publication by Agnieszka T. Kawashima et al. The main goal of this paper was to identify cell cycle dependent regulation of PHLPP1 and its interaction with mitotic proteins. Alexandra Newton is the corresponding author of the manuscript (anewton@health.ucsd.edu); Anne-Claude Gingras should be contacted for questions on this dataset (gingras@lunenfeld.ca).

INSTRUMENT(S): TripleTOF 6600

ORGANISM(S): Homo Sapiens (ncbitaxon:9606)

SUBMITTER: Anne-Claude Gingras  

PROVIDER: MSV000085628 | MassIVE | Wed Jun 24 10:58:00 BST 2020

SECONDARY ACCESSION(S): PXD020003

REPOSITORIES: MassIVE

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Publications

The PHLPP1 N-Terminal Extension Is a Mitotic Cdk1 Substrate and Controls an Interactome Switch.

Kawashima Agnieszka T AT   Wong Cassandra C   Lordén Gema G   King Charles C CC   Lara-Gonzalez Pablo P   Desai Arshad A   Gingras Anne-Claude AC   Newton Alexandra C AC  

Molecular and cellular biology 20210104 3

PH domain leucine-rich repeat protein phosphatase 1 (PHLPP1) is a tumor suppressor that directly dephosphorylates a wide array of substrates, most notably the prosurvival kinase Akt. However, little is known about the molecular mechanisms governing PHLPP1 itself. Here, we report that PHLPP1 is dynamically regulated in a cell cycle-dependent manner and deletion of PHLPP1 results in mitotic delays and increased rates of chromosomal segregation errors. We show that PHLPP1 is hyperphosphorylated dur  ...[more]

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