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MM-1 facilitates degradation of c-Myc by recruiting proteasome and a novel ubiquitin E3 ligase.

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Title: MM-1 facilitates degradation of c-Myc by recruiting proteasome and a novel ubiquitin E3 ligase.
Authors: Kimura, Yumiko Browse this author
Nagao, Arisa Browse this author
Fujioka, Yuko Browse this author
Satou, Akiko Browse this author
Taira, Takahiro Browse this author →KAKEN DB
Iguchi-Ariga, Sanae M M Browse this author →KAKEN DB
Ariga, Hiroyoshi Browse this author →KAKEN DB
Keywords: c-Myc
ubiquitin-proteasome system
Issue Date: Oct-2007
Publisher: D.A. Spandidos
Journal Title: International journal of oncology
Volume: 31
Issue: 4
Start Page: 829
End Page: 836
PMID: 17786314
Abstract: We have reported that a novel c-Myc-binding protein, MM-1, repressed the E-box-dependent transcription activity of c-Myc by recruiting the HDAC1 complex via TIF1beta/KAP1, a transcriptional corepressor. We have also reported that a mutation of A157R in MM-1, which is often observed in patients with leukemia or lymphoma, abrogated all of the repressive activities of MM-1 toward c-Myc, indicating that MM-1 is a novel tumor suppressor. In this study, we found that MM-1 was bound to a component of proteasome and stimulated degradation of c-Myc in human cells. Knockdown of endogenous MM-1 in human HeLa cells by introduction of siRNA against MM-1 stabilized the endogenous c-Myc. To identify proteins that participate in c-Myc degradation by MM-1, in vivo and in vitro binding assays were carried out. The results showed that MM-1 directly bound to Rpt3, a subunit of 26S proteasome, and that c-Myc directly bound to Skp2, which recruited ElonginC, ElonginB and Cullin2, thereby forming a novel ubiquitin E3 ligase. Knockdown of endogenous Cullin2 stabilized the endogenous c-Myc. Thus, MM-1 is a factor that connects c-Myc to the ubiquitin E3 ligase and the proteasome.
Type: article
Appears in Collections:薬学研究院 (Faculty of Pharmaceutical Sciences) > 雑誌発表論文等 (Peer-reviewed Journal Articles, etc)

Submitter: 有賀 寛芳

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