Journal
MOLECULAR & CELLULAR PROTEOMICS
Volume 7, Issue 1, Pages 35-45Publisher
AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
DOI: 10.1074/mcp.M700353-MCP200
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Funding
- NCRR NIH HHS [U54 RR020839-036282, U54 RR020839, U54 RR020839-056887, U54 RR020839-045921, U54RR020839, U54 RR020839-028113] Funding Source: Medline
- NEI NIH HHS [EY015684, R03 EY015684, R03 EY015684-01, R03 EY015684-03, R03 EY015684-02] Funding Source: Medline
- NIGMS NIH HHS [R37 GM028470, R01 GM028470, GM28470] Funding Source: Medline
- NATIONAL CENTER FOR RESEARCH RESOURCES [U54RR020839] Funding Source: NIH RePORTER
- NATIONAL EYE INSTITUTE [R03EY015684] Funding Source: NIH RePORTER
- NATIONAL INSTITUTE OF GENERAL MEDICAL SCIENCES [R01GM028470, R37GM028470] Funding Source: NIH RePORTER
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Ubiquitination is one of the most prevalent protein post-translational modifications in eukaryotes, and its malfunction is associated with a variety of human diseases. Despite the significance of this process, the molecular mechanisms that govern the regulation of ubiquitination remain largely unknown. Here we used a combination of yeast proteome chip assays, genetic screening, and in vitro/in vivo biochemical analyses to identify and characterize eight novel in vivo substrates of the ubiquitinating enzyme Rsp5, a homolog of the human ubiquitin-ligating enzyme Nedd4, in yeast. Our analysis of the effects of a deubiquitinating enzyme, Ubp2, demonstrated that an accumulation of Lys-63-linked polyubiquitin chains results in processed forms of two substrates, Sla1 and Ygr068c. Finally we showed that the localization of another newly identified substrate, Rnr2, is Rsp5-dependent. We believe that our approach constitutes a paradigm for the functional dissection of an enzyme with pleiotropic effects.
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