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Please use this identifier to cite or link to this item: http://ntour.ntou.edu.tw:8080/ir/handle/987654321/45545

Title: Ubc9 acetylation modulates distinct SUMO target modification and hypoxia response.
Authors: Yung‐Lin Hsieh;Hong‐Yi Kuo;Che‐Chang Chang;Mandar T Naik;Pei‐Hsin Liao;Chun‐Chen Ho;Tien‐Chi Huang;Jen‐Chong Jeng;Pang‐Hung Hsu;Ming‐Daw Tsai;Tai‐Huang Huang;Hsiu‐Ming Shih
Contributors: 國立臺灣海洋大學:生命科學系
Date: 2013
Issue Date: 2018-03-26T05:47:21Z
Publisher: The EMBO Journal
Abstract: Abstract: 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) consisting of clustered acidic residues located downstream from the core ψ‐K‐X‐E/D consensus motif, such as CBP and Elk‐1, but not substrates with core ψ‐K‐X‐E/D motif alone or SUMO‐interacting motif. Ubc9 is acetylated at residue K65 and K65 acetylation attenuates Ubc9 binding to NDSM substrates, causing a reduction in NDSM substrate sumoylation. Furthermore, Ubc9 K65 acetylation can be downregulated by hypoxia via SIRT1, and is correlated with hypoxia‐elicited modulation of sumoylation and target gene expression of CBP and Elk‐1 and cell survival. Our data suggest that Ubc9 acetylation/deacetylation serves as a dynamic switch for NDSM substrate sumoylation and we report a previously undescribed SIRT1/Ubc9 regulatory axis in the modulation of protein sumoylation and the hypoxia response.
Relation: 32(6)
URI: http://ntour.ntou.edu.tw:8080/ir/handle/987654321/45545
Appears in Collections:[生命科學系] 期刊論文

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