PXD010822-2

PXD010822 is an original dataset announced via ProteomeXchange.

Title	Stress-induced changes in the S-palmitoylation and S-nitrosylation of proteins involved in synaptic plasticity
Description	Summary The precise regulation of synaptic integrity is critical for neuronal network connectivity and proper brain function. Essential aspects of the activity and localization of synaptic proteins are regulated by posttranslational modifications. S-palmitoylation is a reversible covalent modification of the cysteine with palmitate. It modulates affinity of the protein for cell membranes and membranous compartments. Intracellular palmitoylation dynamics are regulated by other posttranslational modifications, such as S-nitrosylation. Still unclear, however, are the ways in which this crosstalk is affected in brain pathology, such as stress-related disorders. Using a newly developed mass spectrometry-based approach (Palmitoylation And Nitrosylation Interplay Monitoring), we analyzed the endogenous S-palmitoylation and S-nitrosylation of postsynaptic density proteins at the level of specific single cysteines in a mouse model of chronic stress. Our results suggest that atypical mechanism of crosstalk between the S-palmitoylation and S-nitrosylation of synaptic proteins might be one of the major events associated with chronic stress disorders.
HostingRepository	PRIDE
AnnounceDate	2019-07-16
AnnouncementXML	Submission_2019-07-18_03:40:28.xml
DigitalObjectIdentifier
ReviewLevel	Peer-reviewed dataset
DatasetOrigin	Original dataset
RepositorySupport	Unsupported dataset by repository
PrimarySubmitter	Monika Zareba-Koziol
SpeciesList	scientific name: Mus musculus (Mouse); NCBI TaxID: 10090;
ModificationList	N-ethylmaleimide derivatized cysteine; monohydroxylated residue; iodoacetamide derivatized residue
Instrument	Q Exactive

Revision	Datetime	Status	ChangeLog Entry
0	2018-08-20 02:25:38	ID requested
1	2019-07-16 00:38:50	announced
⏵ 2	2019-07-18 03:40:29	announced	Updated publication reference for PubMed record(s): 31311849.
3	2024-10-22 04:13:26	announced	2024-10-22: Updated project metadata.

Zareba-Koziol M, Bartkowiak-Kaczmarek A, Figiel I, Krzystyniak A, Wojtowicz T, Bijata M, Wlodarczyk J, Stress-induced Changes in the S-palmitoylation and S-nitrosylation of Synaptic Proteins. Mol Cell Proteomics, 18(10):1916-1938(2019) [pubmed]

curator keyword: Biological, Biomedical

submitter keyword: PTM's interplay, postsynaptic density synapse, cell signaling, nitrosylation palmitoylation, mass spectrometry

Jakub M Wlodarczyk
contact affiliation	Laboratory of Cell Biophysics, Nencki Institute of Experimental Biology,Polish Academy of Sciences, Warsaw, Poland
contact email	j.wlodarczyk@nencki.gov.pl
lab head
Monika Zareba-Koziol
contact affiliation	Laboratory of Cell Biophysics, Nencki Institute of Experimental Biology, PAS
contact email	m.zareba-koziol@nencki.gov.pl
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/2019/07/PXD010822

PRIDE project URI

• PRIDE
  1. PXD010822
     1. Label: PRIDE project
     2. Name: Stress-induced changes in the S-palmitoylation and S-nitrosylation of proteins involved in synaptic plasticity