PXD025878

PXD025878 is an original dataset announced via ProteomeXchange.

Title	Phosphorylation of Hsp90 on serine residues in the charged linker modulates binding to interacting proteins and has implications for overall Hsp90β conformation (limited proteolysis experiment)
Description	The charged linker region in Hsp90 has been shown to be important for Hsp90 function and global conformation. In humans, two serines located in the charged linker region are constitutively phosphorylated in vivo. In order to gain knowledge on the possible effect of these phosphorylation sites on Hsp90 global conformation, we purified a human Hsp90β mutant where both serines are mutated to alanines, and used limited proteolysis to study the “proteolytic” fingerprint of our mutant and the wild-type, phosphorylated Hsp90β. We observed that serine to alanine mutation resulted in increased tryptic cleavage in the C-domain of Hsp90β.
HostingRepository	PRIDE
AnnounceDate	2021-07-07
AnnouncementXML	Submission_2021-07-06_23:49:56.487.xml
DigitalObjectIdentifier	https://dx.doi.org/10.6019/PXD025878
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; monohydroxylated residue
Instrument	Q Exactive HF

Revision	Datetime	Status	ChangeLog Entry
0	2021-05-07 06:54:54	ID requested
⏵ 1	2021-07-06 23:49:56	announced

Dataset with its publication pending

submitter keyword: Hsp90, limited proteolysis, charged linker, phosphorylation

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. PXD025878
     1. Label: PRIDE project
     2. Name: Phosphorylation of Hsp90 on serine residues in the charged linker modulates binding to interacting proteins and has implications for overall Hsp90β conformation (limited proteolysis experiment)