PXD038701-1

PXD038701 is an original dataset announced via ProteomeXchange.

Title	SUMOylation of Protein Phosphatase 5 Regulates Phosphatase Activity and Substrate Release
Description	The serine/threonine protein phosphatase 5 (PP5) regulates hormone and stress-induced signaling networks. PP5 has been suggested to exist largely in a ‘closed’ and autoinhibitory state whereas the ‘open’ conformation is required for activity. Additionally, PP5 is subject to post-translational modification (PTMs), however, the impact of PTMs on PP5 conformation, activity, and substrate release in cells remains elusive. Here we identified that SUMOylation of K430 in the catalytic domain of PP5 facilitates substrate release. Phosphorylation of PP5-T362 and activation is pre-requisite for SUMOylation suggesting the ordered addition of PTMs carefully regulates PP5 function in cells. Additionally, our quantitative Förster Resonance Energy Transfer (FRET) in live mammalian cells showed that phosphorylation and SUMOylation of PP5 favor a ‘closed’ conformation that functionally is quite different from the autoinhibitory state of PP5. This suggests that PP5 samples multiple conformational states within a cell as a result of PTMs, which do not necessarily correlate with PP5 activity. Furthermore, comparative proteomic analysis of PP5-WT and K430R identified many new potential substrates of PP5. Taken together, our data presented here demonstrate a crucial regulatory step of PP5 activity, SUMOylation of K430R. Notably, the characteristics of a non-SUMOylatable PP5 mutant, K430R, allow rapid identification of new PP5 substrates.
HostingRepository	PRIDE
AnnounceDate	2023-09-08
AnnouncementXML	Submission_2023-09-08_14:18:08.695.xml
DigitalObjectIdentifier
ReviewLevel	Peer-reviewed dataset
DatasetOrigin	Original dataset
RepositorySupport	Unsupported dataset by repository
PrimarySubmitter	SarahBacke
SpeciesList	scientific name: Homo sapiens (Human); NCBI TaxID: 9606;
ModificationList	No PTMs are included in the dataset
Instrument	Orbitrap Fusion Lumos

Revision	Datetime	Status	ChangeLog Entry
0	2022-12-08 16:44:19	ID requested
⏵ 1	2023-09-08 14:18:09	announced
2	2024-10-22 06:02:57	announced	2024-10-22: Updated project metadata.

Dataset with its publication pending

submitter keyword: Chaperone, Ulk1, Chaperone code, Hsp90, ATG1,Autophagy, Phosphorylation

MehdiMollapour
contact affiliation	Department of Urology, SUNY Upstate Medical University Syracuse, NY 13210, US
contact email	mollapom@upstate.edu
lab head
SarahBacke
contact affiliation	SUNY Upstate Medical University
contact email	backes@upstate.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/2023/09/PXD038701

PRIDE project URI

• PRIDE
  1. PXD038701
     1. Label: PRIDE project
     2. Name: SUMOylation of Protein Phosphatase 5 Regulates Phosphatase Activity and Substrate Release