PXD009777

PXD009777 is an original dataset announced via ProteomeXchange.

Title	Cross-linking Analysis (HSP70-HSP90-CHIP)
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 in concert with the cochaperone CHIP –an E3 ligase–, direct their bound substrate to degradation through ubiquitination. 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	2019-03-06
AnnouncementXML	Submission_2019-04-03_07:20:11.xml
DigitalObjectIdentifier
ReviewLevel	Peer-reviewed dataset
DatasetOrigin	Original dataset
RepositorySupport	Unsupported dataset by repository
PrimarySubmitter	Miguel Marcilla
SpeciesList	scientific name: Homo sapiens (Human); NCBI TaxID: 9606;
ModificationList	No PTMs are included in the dataset
Instrument	Orbitrap Fusion Lumos; TripleTOF 5600

Revision	Datetime	Status	ChangeLog Entry
0	2018-05-14 08:19:10	ID requested
1	2019-03-06 00:47:36	announced
⏵ 2	2019-04-03 07:20:12	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]

curator keyword: Biological

submitter keyword: DTSSP, HSP70, HSP90, CHIP

Fernando Corrales
contact affiliation	Proteomics Unit. Macromolecular Structures Department. Spanish National Biotechnology Centre.
contact email	fcorrales@cnb.csic.es
lab head
Miguel Marcilla
contact affiliation	Proteomics Unit - Dpt. of Macromolecular Structures - Spanish National Biotechnolgy Centre (CNB-CSIC)
contact email	mmarcilla@cnb.csic.es
dataset submitter

Dataset FTP location NOTE: Most web browsers have now discontinued native support for FTP access within the browser window. But you can usually install another FTP app (we recommend FileZilla) and configure your browser to launch the external application when you click on this FTP link. Or otherwise, launch an app that supports FTP (like FileZilla) and use this address: ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2019/03/PXD009777

PRIDE project URI

• PRIDE
  1. PXD009777
     1. Label: PRIDE project
     2. Name: Cross-linking Analysis (HSP70-HSP90-CHIP)