Proteomics

Dataset Information

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Quantitative proteomic analysis of proteasome in response to MG132


ABSTRACT: The ubiquitin-proteasome system and autophagy are two major intracellular proteolytic pathways and both remove misfolded and proteotoxic proteins from eukaryotic cells. This study describes the detailed informations about the change in composition and interactome of proteasomes after prolonged MG132 treatment.

INSTRUMENT(S): Q Exactive Plus

ORGANISM(S): Homo Sapiens (human)

TISSUE(S): Embryonic Cell, Kidney

SUBMITTER: Dohyun Han  

LAB HEAD: Dohyun Han

PROVIDER: PXD019193 | Pride | 2021-09-09

REPOSITORIES: Pride

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Publications

Aggresomal sequestration and STUB1-mediated ubiquitylation during mammalian proteaphagy of inhibited proteasomes.

Choi Won Hoon WH   Yun Yejin Y   Park Seoyoung S   Jeon Jun Hyoung JH   Lee Jeeyoung J   Lee Jung Hoon JH   Yang Su-A SA   Kim Nak-Kyoon NK   Jung Chan Hoon CH   Kwon Yong Tae YT   Han Dohyun D   Lim Sang Min SM   Lee Min Jae MJ  

Proceedings of the National Academy of Sciences of the United States of America 20200728 32


The 26S proteasome, a self-compartmentalized protease complex, plays a crucial role in protein quality control. Multiple levels of regulatory systems modulate proteasomal activity for substrate hydrolysis. However, the destruction mechanism of mammalian proteasomes is poorly understood. We found that inhibited proteasomes are sequestered into the insoluble aggresome via HDAC6- and dynein-mediated transport. These proteasomes colocalized with the autophagic receptor SQSTM1 and cleared through sel  ...[more]

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