Proteomics

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Quantitative chemical proteomic profiling of phosphoprotein phosphatases

ABSTRACT: We have developed a chemical proteomic strategy for the systematic interrogation of endogenous phosphoprotein phosphatases (PPP) and their interacting proteins, including regulatory and scaffolding subunits, and substrates (the 'PPPome'). PPPs are captured using an immobilized non-selective PPP inhibitor, followed by identification and quantification by mass spectrometry. Using this approach, we map the PPPome in human cancer cell lines, mouse tissues, and yeast species, identify cell and tissue type specific PPP expression patterns, and discover new PPP interacting proteins.

INSTRUMENT(S): Orbitrap Fusion, Q Exactive Plus

ORGANISM(S): Neurospora Crassa (ncbitaxon:5141) Candida Albicans (ncbitaxon:5476) Saccharomyces Cerevisiae (ncbitaxon:4932) Homo Sapiens (ncbitaxon:9606) Mus Musculus (ncbitaxon:10090) Schizosaccharomyces Pombe (ncbitaxon:4896)

SUBMITTER: Arminja Kettenbach  

PROVIDER: MSV000081226 | MassIVE | Fri Jul 07 07:50:00 BST 2017

SECONDARY ACCESSION(S): PXD006902

REPOSITORIES: MassIVE

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Publications

A Quantitative Chemical Proteomic Strategy for Profiling Phosphoprotein Phosphatases from Yeast to Humans.

Lyons Scott P SP   Jenkins Nicole P NP   Nasa Isha I   Choy Meng S MS   Adamo Mark E ME   Page Rebecca R   Peti Wolfgang W   Moorhead Greg B GB   Kettenbach Arminja N AN  

Molecular & cellular proteomics : MCP 20180918 12

A "tug-of-war" between kinases and phosphatases establishes the phosphorylation states of proteins. While serine and threonine phosphorylation can be catalyzed by more than 400 protein kinases, the majority of serine and threonine dephosphorylation is carried out by seven phosphoprotein phosphatases (PPPs). The PPP family consists of protein phosphatases 1 (PP1), 2A (PP2A), 2B (PP2B), 4 (PP4), 5 (PP5), 6 (PP6), and 7 (PP7). The imbalance in numbers between serine- and threonine-directed kinases  ...[more]

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