Ubc9 acetylation modulates distinct SUMO target modification and hypoxia response
نویسندگان
چکیده
منابع مشابه
Ubc9 acetylation modulates distinct SUMO target modification and hypoxia response.
While numerous small ubiquitin-like modifier (SUMO) conjugated substrates have been identified, very little is known about the cellular signalling mechanisms that differentially regulate substrate sumoylation. Here, we show that acetylation of SUMO E2 conjugase Ubc9 selectively downregulates the sumoylation of substrates with negatively charged amino acid-dependent sumoylation motif (NDSM) cons...
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The ubiquitin-related modifier SUMO regulates a wide range of cellular processes by post-translational modification with one, or a chain of SUMO molecules. Sumoylation is achieved by the sequential action of several enzymes in which the E2, Ubc9, transfers SUMO from the E1 to the target mostly with the help of an E3 enzyme. In this process, Ubc9 not only forms a thioester bond with SUMO, but al...
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In contrast to the dozens of proteins involved in ubiquitination pathways, relatively few proteins control SUMO modification. Generating specificity and diversity in pathway outcomes may therefore rely on post-translational modification of pathway components and/or substrates. A new paper in The EMBO Journal identifies one such modification event, the acetylation of Ubc9, as a key regulatory st...
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Small ubiquitin-related modifier (SUMO) family proteins function by becoming covalently attached to other proteins as post-translational modifications. SUMO modifies many proteins that participate in diverse cellular processes, including transcriptional regulation, nuclear transport, maintenance of genome integrity, and signal transduction. Reversible attachment of SUMO is controlled by an enzy...
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ژورنال
عنوان ژورنال: The EMBO Journal
سال: 2013
ISSN: 0261-4189,1460-2075
DOI: 10.1038/emboj.2013.5