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Molecular & Cellular Proteomics 7:35-45, 2008.
© 2008 by The American Society for Biochemistry and Molecular Biology, Inc.

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Research

Functional Dissection of a HECT Ubiquitin E3 Ligase^*,S

Jin-ying Lu^,,¶,||,**,, Yu-yi Lin^,**,, Jiang Qian^¶¶, Sheng-ce Tao^,, Jian Zhu^,, Cecile Pickart and Heng Zhu^,,||||

From the Departments of Pharmacology and Molecular Sciences, Molecular Biology and Genetics, and ^¶¶ Ophthalmology and The High Throughput Biology Center, The Johns Hopkins University School of Medicine, Baltimore, Maryland 21205 and ^¶ Department of Laboratory Medicine, National Taiwan University Hospital and ^|| Graduate Institute of Clinical Medicine, College of Medicine, National Taiwan University, Taipei 100, Taiwan

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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