التفاصيل البيبلوغرافية
| العنوان: |
MM-1 facilitates degradation of c-Myc by recruiting proteasome and a novel ubiquitin E3 ligase. |
| المؤلفون: |
Kimura, Yumiko, Nagao, Arisa, Fujioka, Yuko, Satou, Akiko, Taira, Takahiro, Iguchi-Ariga, Sanae M M, Ariga, Hiroyoshi |
| بيانات النشر: |
D.A. Spandidos |
| المجموعة: |
Hokkaido University Collection of Scholarly and Academic Papers (HUSCAP) / 北海道大学学術成果コレクション |
| مصطلحات موضوعية: |
c-Myc, MM-1, degradation, ubiquitin-proteasome system, Cullin Proteins/antagonists & inhibitors, Cullin Proteins/genetics, Cullin Proteins/metabolism, HeLa Cells, Humans, Proteasome Endopeptidase Complex/metabolism, Proto-Oncogene Proteins c-myc/genetics, Proto-Oncogene Proteins c-myc/metabolism, RNA, Small Interfering/pharmacology, Repressor Proteins/antagonists & inhibitors, Repressor Proteins/genetics, Repressor Proteins/metabolism, S-Phase Kinase-Associated Proteins/genetics, S-Phase Kinase-Associated Proteins/metabolism, Transcription Factors/genetics, Transcription Factors/metabolism, Transcription, Genetic, Ubiquitin/metabolism, Ubiquitin-Protein Ligases/metabolism |
| الوقت: |
499 |
| الوصف: |
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. |
| نوع الوثيقة: |
article in journal/newspaper |
| اللغة: |
English |
| العلاقة: |
http://hdl.handle.net/2115/53727Test; International journal of oncology, 31(4): 829-836 |
| الإتاحة: |
http://hdl.handle.net/2115/53727Test |
| رقم الانضمام: |
edsbas.370DD6C5 |
| قاعدة البيانات: |
BASE |
