Proteomics

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TRRAP-interacting proteins during heat shock


ABSTRACT: Project description: HeLa cells and cells stably expressing hTRRAP-3xFlAG were subjected to mass spectrometry (MS) analysis. Briefly, Cells were treated or untreated with heat shock at 42°C for 30 min, and TRRAP was immunoprecipitated from these cell extracts with 60 ul anti-FLAG M2 affinity gels by rotating at 4°C for 3 h. Immunoprecipitated sample was eluted by 40 ul FLAG peptide at 4°C for 30 min. Protein samples were loaded on 12% SDS-PAGE for preparation of gel slices. Gel bands were cut-out and subjected to in-gel digestion with trypsin. Resulting peptides were dissolved in a solution containing 0.1% trifluoroacetic acid and 2% acetonitrile and analyzed by an LTQ Orbitrap Velos Pro mass spectrometer coupled with a nanoLC instrument and HTC-PAL autosampler.

ORGANISM(S): Homo Sapiens (human)

SUBMITTER: Nakai Akira 

PROVIDER: PXD031822 | JPOST Repository | Sun Jun 19 00:00:00 GMT+01:00 2022

REPOSITORIES: jPOST

Dataset's files

Source:
Action DRS
orb_190624_AE-MF-7_%231-1.raw Raw
orb_190624_AE-MF-7_%231-2.raw Raw
orb_190624_AE-MF-7_%231-3.raw Raw
orb_190624_AE-MF-7_%231-4.raw Raw
orb_190624_AE-MF-7_%231-5.raw Raw
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Publications

HSF1 phosphorylation establishes an active chromatin state via the TRRAP-TIP60 complex and promotes tumorigenesis.

Fujimoto Mitsuaki M   Takii Ryosuke R   Matsumoto Masaki M   Okada Mariko M   Nakayama Keiich I KI   Nakato Ryuichiro R   Fujiki Katsunori K   Shirahige Katsuhiko K   Nakai Akira A  

Nature communications 20220729 1


Transcriptional regulation by RNA polymerase II is associated with changes in chromatin structure. Activated and promoter-bound heat shock transcription factor 1 (HSF1) recruits transcriptional co-activators, including histone-modifying enzymes; however, the mechanisms underlying chromatin opening remain unclear. Here, we demonstrate that HSF1 recruits the TRRAP-TIP60 acetyltransferase complex in HSP72 promoter during heat shock in a manner dependent on phosphorylation of HSF1-S419. TRIM33, a br  ...[more]

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