PXD025888

PXD025888 is an original dataset announced via ProteomeXchange.

Title	Phosphorylation of Hsp90β on serine residues in the charged linker modulates binding to interacting proteins and has implications for overall Hsp90β conformation (Occupancy and phospho-modulation data)
Description	Human Hsp90β is constitutively phosphorylated in vivo on two serine residues in the charged linker region, S226 and S255. We developed a targeted method to measure the phosphorylation occupancy (the extent of phosphorylation) of both phosphosites in a range of cultured cell lines and consistently found high occupancy (>90%) in the cytoplasm and nucleus. However, we found decreased phosphorylation, especially for S255, in Hsp90β purified from the conditioned medium of cultured K562 cells. In addition, we investigated if various cell growth conditions known to impact Hsp90β activity had an effect on the phosphorylation status of S226 and S255, but none of the conditions tested (e.g. heat shock, Hsp90β inhibition) resulted in an alteration of S226 and S255 phosphorylation.
HostingRepository	PRIDE
AnnounceDate	2021-07-07
AnnouncementXML	Submission_2021-07-06_23:34:08.389.xml
DigitalObjectIdentifier	https://dx.doi.org/10.6019/PXD025888
ReviewLevel	Peer-reviewed dataset
DatasetOrigin	Original dataset
RepositorySupport	Supported dataset by repository
PrimarySubmitter	Manfredo Quadroni
SpeciesList	scientific name: Homo sapiens (Human); NCBI TaxID: 9606;
ModificationList	phosphorylated residue
Instrument	Orbitrap Fusion

Revision	Datetime	Status	ChangeLog Entry
0	2021-05-07 09:46:39	ID requested
⏵ 1	2021-07-06 23:34:08	announced

Dataset with its publication pending

submitter keyword: Hsp90, phosphorylation, occupancy, TiO, heat shock, stress, Hsp90 inhibitors

Manfredo Quadroni
contact affiliation	Protein Analysis Facility, Faculty of Biology and Medicine, University of Lausanne, Switzerland
contact email	manfredo.quadroni@unil.ch
lab head
Manfredo Quadroni
contact affiliation	University of Lausanne
contact email	manfredo.quadroni@unil.ch
dataset submitter

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PRIDE project URI

• PRIDE
  1. PXD025888
     1. Label: PRIDE project
     2. Name: Phosphorylation of Hsp90β on serine residues in the charged linker modulates binding to interacting proteins and has implications for overall Hsp90β conformation (Occupancy and phospho-modulation data)