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Article

Quantitative phosphoproteomics reveals pathways for coordination of cell growth and division by the conserved fission yeast kinase pom1.

Molecular & cellular proteomics : MCP - 1 May 2015

Kettenbach Arminja N, Deng Lin, Wu Youjun, Baldissard Suzanne, Adamo Mark E, Gerber Scott A, Moseley James B

Abstract excerpt

Complex phosphorylation-dependent signaling networks underlie the coordination of cellular growth and division. In the fission yeast Schizosaccharomyces pombe, the Dual specificity tyrosine-(Y)-phosphorylation regulated kinase (DYRK) family protein kinase Pom1 regulates cell cycle progression through the mitotic inducer Cdr2 and controls cell polarity through unknown targets. Here, we sought to determine the...

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PMID: 25720772
DOI: 10.1074/mcp.M114.045245
PMCID: PMC4424399

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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Quantitative phosphoproteomics reveals pathways for coordination of cell growth and division by the conserved fission yeast kinase pom1.PMID 25720772Read ↗

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