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

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          Abstract

          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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          Author and article information

          Journal
          Mol. Cell Proteomics
          Molecular & cellular proteomics : MCP
          1535-9484
          1535-9476
          Dec 2015
          : 14
          : 12
          Affiliations
          [1 ] From the Cell & Developmental Biology, Vanderbilt University School of Medicine, 1161 21st Avenue South, Nashville, TN 37232.
          [2 ] Departments of Structural Biology and Developmental Neurobiology, St. Jude Proteomics Facility, St. Jude Children's Research Hospital, Memphis, TN 38105.
          [3 ] From the Cell & Developmental Biology, Vanderbilt University School of Medicine, 1161 21st Avenue South, Nashville, TN 37232 kathy.gould@vanderbilt.edu.
          Article
          M115.050039
          10.1074/mcp.M115.050039
          26412298
          © 2015 by The American Society for Biochemistry and Molecular Biology, Inc.

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