A genome-wide synthetic dosage lethality screen reveals multiple pathways that require the functioning of ubiquitin-binding proteins Rad23 and Dsk2 |
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Authors: | Chang Liu Dewald van Dyk Yue Li Brenda Andrews Hai Rao |
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Institution: | (1) Department of Molecular Medicine, Institute of Biotechnology, University of Texas Health Science Center at San Antonio, San Antonio, Texas 78245, USA;(2) Banting & Best Department of Medical Research, Department of Molecular & Medical Genetics, University of Toronto, Toronto, Ontario, Canada |
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Abstract: | Background Ubiquitin regulates a myriad of important cellular processes through covalent attachment to its substrates. A classic role
for ubiquitin is to flag proteins for destruction by the proteasome. Recent studies indicate that ubiquitin-binding proteins
(e.g. Rad23, Dsk2, Rpn10) play a pivotal role in transferring ubiquitylated proteins to the proteasome. However, the specific
role of these ubiquitin receptors remains poorly defined. A key to unraveling the functions of these ubiquitin receptors is
to identify their cellular substrates and biological circuits they are involved in. Although many strategies have been developed
for substrate isolation, the identification of physiological targets of proteolytic pathways has proven to be quite challenging. |
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