SUMOylation of Psmd1 Controls Adrm1 Interaction with the Proteasome
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Issue Date
2014-06-05Author
Ryu, Hyunju
Gygi, Steven P.
Azuma, Yoshiaki
Arnaoutov, Alexei
Dasso, Mary
Publisher
Elsevier
Type
Article
Article Version
Scholarly/refereed, publisher version
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Show full item recordAbstract
SUMOylation is the covalent conjugation of SUMO polypeptides to cellular target proteins. Psmd1 is a subunit of the proteasomal 19S regulatory particle that acts as a docking site for Adrm1, another proteasome subunit that recruits ubiquitinated substrates for proteolysis. Here, we show that the SUMO deconjugating enzyme xSENP1 specifically interacts with Psmd1 and that disruption of xSENP1 targeting delays mitotic exit. Psmd1 becomes SUMOylated through the action of the SUMO E3 enzyme PIASy. We mapped SUMOylation sites within Psmd1 and found that SUMOylation of a critical lysine immediately adjacent to the Adrm1-binding domain regulates the association of Adrm1 with Psmd1. Together, our findings suggest that the interaction of Psmd1 with Adrm1 is controlled by SUMOylation in a manner that may alter proteasome composition and function. These findings demonstrate a mechanism for regulation of ubiquitin-mediated protein degradation by ubiquitin-like proteins of the SUMO family.
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This is the published version. This is an open access article under the CC BY license (http://creativecommons.org/licenses/by/3.0/).
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Citation
Ryu, Hyunju, Steven P. Gygi, Yoshiaki Azuma, Alexei Arnaoutov, and Mary Dasso. "SUMOylation of Psmd1 Controls Adrm1 Interaction with the Proteasome." Cell Reports 7.6 (2014): 1842-848. Elsevier. http://dx.doi.org/10.1016/j.celrep.2014.05.009
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