Proteomics

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Discovery of human breast cancer cell MCF7 heat induced proteins by LC-MS/MS

ABSTRACT: Co-translational degradation via the ubiquitin-proteasome system mediates quality control of 15 – 25% of nascent proteins, a proportion that is known to increase dramatically under proteotoxic stress conditions. Whereas the ubiquitylation machinery involved has been characterized, mechanisms coordinating the proteasomal destruction of ribosome-attached nascent proteins remain poorly defined. In pursuit of such mechanisms, we discovered dual cooperation of the HSP70 family member HSPA1 with the 26S proteasome: First, in response to proteotoxic stress, HSPA1 promotes proteasome recruitment to translating 80S ribosomes in a manner independent of nascent chain ubiquitylation. Secondly, HSPA1, in association with its cognate nucleotide exchange factor HSPH1, maintains co-translationally ubiquitylated proteins in a soluble state required for efficient proteasomal degradation.

INSTRUMENT(S): Q Exactive

ORGANISM(S): Homo Sapiens (human)

TISSUE(S): Cell Culture

SUBMITTER: Guiyou Tian  

LAB HEAD: Dieter A.Wolf

PROVIDER: PXD020140 | Pride | 2021-09-09

REPOSITORIES: Pride

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Dual roles of HSP70 chaperone HSPA1 in quality control of nascent and newly synthesized proteins.

Tian Guiyou G   Hu Cheng C   Yun Yun Y   Yang Wensheng W   Dubiel Wolfgang W   Cheng Yabin Y   Wolf Dieter A DA  

The EMBO journal 20210519 13

Exposure to heat stress triggers a well-defined acute response marked by HSF1-dependent transcriptional upregulation of heat shock proteins. Cells allowed to recover acquire thermotolerance, but this adaptation is poorly understood. By quantitative proteomics, we discovered selective upregulation of HSP70-family chaperone HSPA1 and its co-factors, HSPH1 and DNAJB1, in MCF7 breast cancer cells acquiring thermotolerance. HSPA1 was found to have dual function during heat stress response: (i) During  ...[more]

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