PXD008375-2

PXD008375 is an original dataset announced via ProteomeXchange.

Title	Cdc37 and Hsp90 tyrosine phosphorylation modulate the kinase chaperone cycle
Description	Cdc37 is a core cochaperone of the Hsp90 machinery. It is involved in an early stage of the chaperone cycle to activate nascent forms of protein kinases as well as to stabilize mature forms of a subset of protein kinases. Overall, the chaperone cycle is quite complex and involves several steps. Progression, through these steps is regulated by the incorporation of several other cochaperones, ATP hydrolysis and posttranslational modifications on both Cdc37 and Hsp90. We show that phosphorylation of Cdc37 at Y298 by Yes kinase results in partial unfolding of its C-terminal domain, without affecting its ability to form binary or ternary complexes with kinases and Hsp90. Unfolding, unmasks a phosphopeptide sequence that exhibits high affinity for SH2 domains of non-receptor tyrosine kinases (nRTKs), resulting in their recruitment in the chaperone complex. In turn, the high local concentration of nRTKs potentiates Hsp90 phosphorylation at Y197, which results in dissociation of this early kinase-recruitment complex
HostingRepository	PRIDE
AnnounceDate	2024-10-22
AnnouncementXML	Submission_2024-10-22_04:42:37.795.xml
DigitalObjectIdentifier
ReviewLevel	Peer-reviewed dataset
DatasetOrigin	Original dataset
RepositorySupport	Unsupported dataset by repository
PrimarySubmitter	Dale Chaput
SpeciesList	scientific name: Homo sapiens (Human); NCBI TaxID: 9606;
ModificationList	phosphorylated residue; monohydroxylated residue; iodoacetamide derivatized residue
Instrument	Q Exactive

Revision	Datetime	Status	ChangeLog Entry
0	2017-12-06 03:44:55	ID requested
1	2018-01-22 03:56:45	announced
⏵ 2	2024-10-22 04:42:46	announced	2024-10-22: Updated project metadata.

10.1038/s41467-017-02711-w;

Bachman AB, Keramisanou D, Xu W, Beebe K, Moses MA, Vasantha Kumar MV, Gray G, Noor RE, van der Vaart A, Neckers L, Gelis I, Phosphorylation induced cochaperone unfolding promotes kinase recruitment and client class-specific Hsp90 phosphorylation. Nat Commun, 9(1):265(2018) [pubmed]

curator keyword: Biological

submitter keyword: Phosphorylation, LC-MS/MS

Dr. Ioannis Gelis
contact affiliation	Assistant Professor Department of Chemisty University of South Florida Tampa, FL. USA.
contact email	igelis@usf.edu
lab head
Dale Chaput
contact affiliation	University of South Florida
contact email	chaput@usf.edu
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/2018/01/PXD008375

PRIDE project URI

• PRIDE
  1. PXD008375
     1. Label: PRIDE project
     2. Name: Cdc37 and Hsp90 tyrosine phosphorylation modulate the kinase chaperone cycle