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Fission yeast DUB substrates - A Degenerate Cohort of Yeast Membrane Trafficking DUBs Mediates Cell Polarity and Survival

ABSTRACT: His-Biotin-His Ubiquitin was overexpressed in various fission yeast (S. pombe) genetic backgrounds to identify ubiqutinated proteins. Normalizing to bait (ubiquitin) across samples provided insight into relative changes in ubiquitination with loss of deubiquitinases (DUBs), yielding putative DUB substrates.

INSTRUMENT(S): LTQ, LTQ Velos

ORGANISM(S): Schizosaccharomyces Pombe

SUBMITTER: Janel Beckley

LAB HEAD: Kathleen L. Gould

PROVIDER: PXD001767 | Pride | 2017-06-09

REPOSITORIES: Pride

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			Action	DRS
	JSC20130325_pREP1UbHBH_0.raw	Raw
	JSC20130325_pREP1UbHBH_10.raw	Raw
	JSC20130325_pREP1UbHBH_100.raw	Raw
	JSC20130325_pREP1UbHBH_1000.raw	Raw
	JSC20130325_pREP1UbHBH_1000p1.raw	Raw

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Publications

A Degenerate Cohort of Yeast Membrane Trafficking DUBs Mediates Cell Polarity and Survival.

Beckley Janel R JR Chen Jun-Song JS Yang Yanling Y Peng Junmin J Gould Kathleen L KL

Molecular & cellular proteomics : MCP 20150927 12

Deubiquitinating enzymes (DUBs), cysteine or metallo- proteases that cleave ubiquitin chains or protein conjugates, are present in nearly every cellular compartment, with overlapping protein domain structure, localization, and functions. We discovered a cohort of DUBs that are involved in membrane trafficking (ubp4, ubp5, ubp9, ubp15, and sst2) and found that loss of all five of these DUBs but not loss of any combination of four, significantly impacted cell viability in the fission yeast Schizos ...[more]

PMID: 26412298

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A Degenerate Cohort of Yeast Membrane Trafficking DUBs Mediates Cell Polarity and Survival.

Project description:Deubiquitinating enzymes (DUBs), cysteine or metallo- proteases that cleave ubiquitin chains or protein conjugates, are present in nearly every cellular compartment, with overlapping protein domain structure, localization, and functions. We discovered a cohort of DUBs that are involved in membrane trafficking (ubp4, ubp5, ubp9, ubp15, and sst2) and found that loss of all five of these DUBs but not loss of any combination of four, significantly impacted cell viability in the fission yeast Schizosaccharomyces pombe (1). Here, we delineate the collective and individual functions and activities of these five conserved DUBs using comparative proteomics, biochemistry, and microscopy. We find these five DUBs are degenerate rather than redundant at the levels of cell morphology, substrate selectivity, ubiquitin chain specificity, and cell viability under stress. These studies reveal the complexity of interplay among these enzymes, providing a foundation for understanding DUB biology and providing another example of how cells utilize degeneracy to improve survival.

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