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Wigington_calcineurinphosphatasesignaling_SWATH_2019

ABSTRACT: The files are associated with a manuscript submitted for publication by Callie P. Wigington et al. The main goal of this paper was to identify how calcineurin (CN) binds substrates via PxIxIT and LxVP motifs, elucidated through short linear motifs (SLiM) discovery.

INSTRUMENT(S): TripleTOF 6600

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

SUBMITTER: Anne-Claude Gingras

PROVIDER: MSV000083697 | MassIVE | Tue Apr 16 08:18:00 BST 2019

SECONDARY ACCESSION(S): PXD013529

REPOSITORIES: MassIVE

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Publications

Systematic Discovery of Short Linear Motifs Decodes Calcineurin Phosphatase Signaling.

Wigington Callie P CP Roy Jagoree J Damle Nikhil P NP Yadav Vikash K VK Blikstad Cecilia C Resch Eduard E Wong Cassandra J CJ Mackay Douglas R DR Wang Jennifer T JT Krystkowiak Izabella I Bradburn Devin A DA Tsekitsidou Eirini E Hong Su Hyun SH Kaderali Malika Amyn MA Xu Shou-Ling SL Stearns Tim T Gingras Anne-Claude AC Ullman Katharine S KS Ivarsson Ylva Y Davey Norman E NE Cyert Martha S MS

Molecular cell 20200708 2

Short linear motifs (SLiMs) drive dynamic protein-protein interactions essential for signaling, but sequence degeneracy and low binding affinities make them difficult to identify. We harnessed unbiased systematic approaches for SLiM discovery to elucidate the regulatory network of calcineurin (CN)/PP2B, the Ca<sup>2+</sup>-activated phosphatase that recognizes LxVP and PxIxIT motifs. In vitro proteome-wide detection of CN-binding peptides, in vivo SLiM-dependent proximity labeling, and in silico ...[more]

PMID: 32645368

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Wigington_calcineurinphosphatasesignaling_2019

Project description:The files are associated with a manuscript submitted for publication by Callie P. Wigington et al. The main goal of this paper was to identify how calcineurin (CN) binds substrates via PxIxIT and LxVP motifs, elucidated through short linear motifs (SLiM) discovery.

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Systematic discovery of Short Linear Motifs decodes calcineurin phosphatase signaling

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