PXD009756

PXD009756 is an original dataset announced via ProteomeXchange.

Title	The cochaperone CHIP marks Hsp70- and Hsp90-bound substrates for degradation through a very flexible mechanism
Description	Some molecular chaperones are involved not only in assisting the folding of proteins but also, given appropriate conditions, in their degradation. This is the case of Hsp70 and Hsp90, which direct their bound substrate to degradation through ubiquitination in concert with the cochaperone CHIP –an E3 ligase. We have generated complexes between the chaperone (Hsp70 or Hsp90), the cochaperone CHIP and, as substrate, a p53 variant containing the GST protein (p53-TMGST). The two ternary complexes (Hsp70:p53-TMGST:CHIP and Hsp90:p53-TMGST:CHIP) ubiquitinate the substrate, and this is done with a higher efficiency than in the absence of the chaperones. The 3D structures of the two complexes, obtained using a combination of cryoelectron microscopy and crosslinking mass spectrometry, show the substrate located between the chaperone and the cochaperone, which suggests an ubiquitination mechanism. Both complexes are extremely flexible, which is crucial for the ubiquitination process.
HostingRepository	PRIDE
AnnounceDate	2019-03-07
AnnouncementXML	Submission_2019-04-03_07:20:39.xml
DigitalObjectIdentifier
ReviewLevel	Peer-reviewed dataset
DatasetOrigin	Original dataset
RepositorySupport	Unsupported dataset by repository
PrimarySubmitter	Eduard Sabidó
SpeciesList	scientific name: Homo sapiens (Human); NCBI TaxID: 9606;
ModificationList	monohydroxylated residue; iodoacetamide derivatized residue
Instrument	Orbitrap Fusion Lumos

Revision	Datetime	Status	ChangeLog Entry
0	2018-05-11 04:56:03	ID requested
1	2019-03-07 02:38:13	announced
⏵ 2	2019-04-03 07:20:40	announced	Updated publication reference for PubMed record(s): 30911017.

Quintana-Gallardo L, Mart, í, n-Benito J, Marcilla M, Espadas G, Sabid, ó E, Valpuesta JM, The cochaperone CHIP marks Hsp70- and Hsp90-bound substrates for degradation through a very flexible mechanism. Sci Rep, 9(1):5102(2019) [pubmed]

submitter keyword: DSSO, crosslinking, shotgun

Eduard Sabidó
contact affiliation	CRG/UPF Proteomics Unit, Center for Genomics Regulation, Universitat Pompeu Fabra, 08003 Barcelona, Spain.
contact email	eduard.sabido@crg.cat
lab head
Eduard Sabidó
contact affiliation	Centre de Regulació Genòmica
contact email	eduard.sabido@crg.cat
dataset submitter

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PRIDE project URI

• PRIDE
  1. PXD009756
     1. Label: PRIDE project
     2. Name: The cochaperone CHIP marks Hsp70- and Hsp90-bound substrates for degradation through a very flexible mechanism