Proteomics

Dataset Information

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The deubiquitinase USP7 stabilizes Maf proteins to promote myeloma cell survival


ABSTRACT: USP7, as a deubiquitination enzyme, controls ubiquitination and stability of Maf family proteins. USP7 promotes Maf transcriptional activity. Moreover, USP7 is overexpressed in multiple myeloma cells and its expression level is negatively correlated to the survival of myeloma patients.

INSTRUMENT(S): Q Exactive

ORGANISM(S): Homo Sapiens (human)

TISSUE(S): Epithelial Cell

DISEASE(S): Multiple Myeloma

SUBMITTER: Jiefei Tong  

LAB HEAD: Mike Moran

PROVIDER: PXD016020 | Pride | 2019-12-16

REPOSITORIES: Pride

Dataset's files

Source:
Action DRS
Biyin-MG1321st.raw Raw
Biyin-MG1322nd.raw Raw
Biyin-MG1323rd.raw Raw
Biyin-MafB1st.raw Raw
Biyin-MafB2nd.raw Raw
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Publications

The deubiquitinase USP7 stabilizes Maf proteins to promote myeloma cell survival.

He Yuanming Y   Wang Siyu S   Tong Jiefei J   Jiang Shuoyi S   Yang Ye Y   Zhang Zubin Z   Xu Yujia Y   Zeng Yuanying Y   Cao Biyin B   Moran Michael F MF   Mao Xinliang X  

The Journal of biological chemistry 20191210 7


The Maf proteins, including c-Maf, MafA, and MafB, are critical transcription factors in myelomagenesis. Previous studies demonstrated that Maf proteins are processed by the ubiquitin-proteasome pathway, but the mechanisms remain elusive. This study applied MS to identify MafB ubiquitination-associated proteins and found that the ubiquitin-specific protease USP7 was present in the MafB interactome. Moreover, USP7 also interacted with c-Maf and MafA and blocked their polyubiquitination and degrad  ...[more]

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