PXD001649

PXD001649 is an original dataset announced via ProteomeXchange.

Title	Pom1-AS quantitative phosphoproteomics
Description	Complex phosphorylation-dependent signaling networks underlie the coordination of cellular growth and division. In the fission yeast S. pombe, the DYRK family protein kinase regulates cell cycle progression through the mitotic inducer Cdr2, and controls cell polarity through unknown targets. Here, we sought to determine the phosphorylation targets of Pom1 kinase activity by SILAC-based phosphoproteomics. We defined a set of high-confidence Pom1 targets that were enriched for cytoskeletal and cell growth functions. Cdr2 was the only cell cycle target of Pom1 kinase activity that we identified in cells. Mutation of Pom1-dependent phosphorylation sites in the C-terminus of Cdr2 inhibited mitotic entry but did not impair Cdr2 localization. In addition, we found that Pom1 phosphorylated multiple substrates that function in polarized cell growth, including Tea4, Mod5, Pal1, the Rho GAP Rga7, and the Arf GEF Syt22. Purified Pom1 phosphorylated these cell polarity targets in vitro, confirming that they are direct substrates of Pom1 kinase activity and likely contribute to regulation of polarized growth by Pom1. Our study demonstrates that Pom1 acts in a linear pathway to control cell cycle progression while regulating a complex network of cell growth targets.
HostingRepository	PRIDE
AnnounceDate	2015-03-09
AnnouncementXML	Submission_2015-03-09_06:27:38.xml
DigitalObjectIdentifier	https://dx.doi.org/10.6019/PXD001649
ReviewLevel	Peer-reviewed dataset
DatasetOrigin	Original dataset
RepositorySupport	Supported dataset by repository
PrimarySubmitter	Scott Gerber
SpeciesList	scientific name: Schizosaccharomyces pombe; NCBI TaxID: 4896;
ModificationList	Oxidation; Phospho; Label:13C(6)15N(4); Carbamidomethyl; Label:13C(6)15N(2)
Instrument	LTQ Orbitrap

Revision	Datetime	Status	ChangeLog Entry
0	2015-01-05 03:28:30	ID requested
⏵ 1	2015-03-09 06:27:41	announced

Kettenbach AN, Deng L, Wu Y, Baldissard S, Adamo ME, Gerber SA, Moseley JB, Quantitative phosphoproteomics reveals pathways for coordination of cell growth and division by the conserved fission yeast kinase pom1. Mol Cell Proteomics, 14(5):1275-87(2015) [pubmed]

curator keyword: Biological

submitter keyword: Pom1, phosphoproteomics, SILAC, pombe

Scott Gerber
contact affiliation	Departments of Genetics and Biochemistry, Geisel School of Medicine at Dartmouth, Lebanon, New Hampshire, USA
contact email	scott.a.gerber@dartmouth.edu
lab head
Scott Gerber
contact affiliation	Dartmouth
contact email	scott.a.gerber@dartmouth.edu
dataset submitter

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PRIDE project URI

• PRIDE
  1. PXD001649
     1. Label: PRIDE project
     2. Name: Pom1-AS quantitative phosphoproteomics