PXD005740

PXD005740 is an original dataset announced via ProteomeXchange.

Title	CALCIUM-DEPENDENT PROTEOLYSIS OF THE ARABIDOPSIS DAMP PRECURSOR PROPEP1 BY THE CYSTEINE PROTEASE METACASPASE4 REVEALS A CONSERVED MECHANISM FOR IMMEDIATE RELEASE OF PEPTIDE SIGNALS DURING WOUND RESPONSES
Description	In animals, one of the most immediate responses to tissue wounding comprises the release of peptide signals such as interleukins from their precursor proteins. Although the wound response has been intensively studied in plants as well, little is known about plant peptides with cytokine-like functions. Here we report that in Arabidopsis thaliana, wounding triggers the instantaneous activation of the METACASPASE4 cysteine protease and subsequent cleavage of the PROPEP1 precursor to release the mature peptide signal PEP1, which induces basal immunity against pathogens. Furthermore, confocal microscopy of targeted cell damage by laser wounding revealed that the inactive zymogen of MC4 and PROPEP1 reside in the cytosol until a constitutive increase in calcium concentration upon cell membrane integrity loss triggers MC4 activation and PROPEP1 cleavage. PROPEP1 cleavage and PEP1 release is restricted to only a few cells surrounding the damaged site. Our results highlight the similarities of the spatiotemporal dynamics and control mechanisms of the plant wound response as an example for convergent evolution with respect to the mammalian system, in which calpain releases IL1-α from its precursor.
HostingRepository	PRIDE
AnnounceDate	2024-10-22
AnnouncementXML	Submission_2024-10-22_04:35:43.230.xml
DigitalObjectIdentifier	https://dx.doi.org/10.6019/PXD005740
ReviewLevel	Peer-reviewed dataset
DatasetOrigin	Original dataset
RepositorySupport	Supported dataset by repository
PrimarySubmitter	An Staes
SpeciesList	scientific name: Arabidopsis thaliana (Mouse-ear cress); NCBI TaxID: 3702;
ModificationList	Oxidation
Instrument	Q Exactive

Revision	Datetime	Status	ChangeLog Entry
0	2017-01-18 05:28:31	ID requested
1	2019-04-23 02:13:40	announced
⏵ 2	2024-10-22 04:35:44	announced	2024-10-22: Updated project metadata.

Hander T, Fern, á, ndez-Fern, á, ndez Á D, Kumpf RP, Willems P, Schatowitz H, Rombaut D, Staes A, Nolf J, Pottie R, Yao P, Gon, ç, alves A, Pavie B, Boller T, Gevaert K, Van Breusegem F, Bartels S, Stael S, -dependent metacaspases for release of immunomodulatory peptides. Science, 363(6433):(2019) [pubmed]

10.1126/science.aar7486;

10.6019/PXD005740;

curator keyword: Biological

submitter keyword: peptidomics, Propep1,Metacaspase,arabidopsis

Kris Gevaert
contact affiliation	Center for Medical Biotechnology, VIB, 9000 Ghent, Belgium Department of Biochemistry, Ghent University, 9000 Ghent, Belgium
contact email	kris.gevaer@vib-ugent.be
lab head
An Staes
contact affiliation	Medical Protein Chemistry
contact email	an.staes@vib-ugent.be
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/2019/04/PXD005740

PRIDE project URI

• PRIDE
  1. PXD005740
     1. Label: PRIDE project
     2. Name: CALCIUM-DEPENDENT PROTEOLYSIS OF THE ARABIDOPSIS DAMP PRECURSOR PROPEP1 BY THE CYSTEINE PROTEASE METACASPASE4 REVEALS A CONSERVED MECHANISM FOR IMMEDIATE RELEASE OF PEPTIDE SIGNALS DURING WOUND RESPONSES