PXD026893

PXD026893 is an original dataset announced via ProteomeXchange.

Title	p53 forms redox-dependent protein-protein interactions through cysteine 277
Description	Reversible cysteine oxidation plays an essential role in redox signaling by reversibly altering protein structure and function. Cysteine oxidation may lead to intra- and intermolecular disulfide formation, and the latter can drastically stabilize protein-protein interactions in a more oxidizing milieu. The activity of the tumor suppressor p53 is regulated at multiple layers, including various post-translational modification (PTM) and protein-protein interactions. In the past decades, p53 has been shown to be a redox sensitive protein, and undergoes reversible cysteine oxidation both in vitro and in vivo. It is not clear however, whether p53 also forms intermolecular disulfides with interacting proteins and whether these redox-dependent interactions contribute to the regulation of p53. In the present study, by combining (co-)immunoprecipitation, quantitative Mass spectrometry and Western blot we found that p53 forms disulfide-dependent interactions with several proteins under oxidizing conditions. p53-Cys277 is required for most of the disulfide-dependent interactions, including those with 14-3-3 and 53BP1. Taken together, our findings uncovered a new form of p53 cysteine oxidation, which strengthened the biochemical features of p53 as a redox sensitive protein.
HostingRepository	PRIDE
AnnounceDate	2021-11-02
AnnouncementXML	Submission_2021-11-02_07:05:32.705.xml
DigitalObjectIdentifier
ReviewLevel	Peer-reviewed dataset
DatasetOrigin	Original dataset
RepositorySupport	Unsupported dataset by repository
PrimarySubmitter	Harmjan Vos
SpeciesList	scientific name: Homo sapiens (Human); NCBI TaxID: 9606;
ModificationList	No PTMs are included in the dataset
Instrument	Orbitrap Fusion

Revision	Datetime	Status	ChangeLog Entry
0	2021-06-23 22:06:31	ID requested
⏵ 1	2021-11-02 07:05:33	announced

Dataset with its publication pending

submitter keyword: p53 redox-dependent protein-protein interactions cysteine

Tobias Dansen
contact affiliation	Department Molecular Cancer Research , Center for Molecular Medicine, Universitair Medisch Centrum Utrecht, The Netherlands
contact email	T.B.Dansen@umcutrecht.nl
lab head
Harmjan Vos
contact affiliation	University Medical Center Utrecht Dept. Molecular Cancer Research
contact email	h.r.vos-3@umcutrecht.nl
dataset submitter

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PRIDE project URI

• PRIDE
  1. PXD026893
     1. Label: PRIDE project
     2. Name: p53 forms redox-dependent protein-protein interactions through cysteine 277