PXD015676

PXD015676 is an original dataset announced via ProteomeXchange.

Title	Phosphorylation of the receptor protein Pex5p modulates import of PTS1 cargoes into peroxisomesPhosphorylation of the receptor protein Pex5p modulates import of PTS1 cargoes into peroxisomes
Description	Peroxisomes are dynamic organelles with vital functions in cellular metabolism and dysfunction of peroxisomes is associated with human diseases. To fulfill their multiple roles, peroxisomes rely on import of nuclear-encoded matrix proteins, most carrying a peroxisomal targeting signal (PTS) 1. The receptor Pex5p recruits PTS1-proteins for import into peroxisomes; whether and how this process is posttranslationally regulated is unknown. Here, we identify 22 phosphorylation sites of Pex5p. Yeast cells expressing phospho-mimicking Pex5p-S507/523D (Pex5p-2D) show a decreased peroxisomal import of GFP-SKL. We show that the binding affinity between PTS1-protein and Pex5p-2D is reduced. An in vivo analysis of the effect of the phosphomimicking mutants on all known PTS1-proteins revealed that import of most, but not all, cargo proteins is affected. The physiological effect of the phosphomimetic mutations correlate with the binding affinity of the corresponding extended PTS1-sequences. Thus, we report a novel Pex5p phosphorylation-dependent mechanism for regulating PTS1-protein import into peroxisomes.
HostingRepository	PRIDE
AnnounceDate	2023-11-14
AnnouncementXML	Submission_2023-11-14_08:05:36.899.xml
DigitalObjectIdentifier
ReviewLevel	Peer-reviewed dataset
DatasetOrigin	Original dataset
RepositorySupport	Unsupported dataset by repository
PrimarySubmitter	Friedel Drepper
SpeciesList	scientific name: Saccharomyces cerevisiae (Baker's yeast); NCBI TaxID: 4932;
ModificationList	phosphorylated residue; monohydroxylated residue; acetylated residue; iodoacetamide derivatized residue
Instrument	Q Exactive

Revision	Datetime	Status	ChangeLog Entry
0	2019-10-02 03:39:32	ID requested
1	2023-03-10 13:01:55	announced
⏵ 2	2023-11-14 08:05:39	announced	2023-11-14: Updated project metadata.

Fischer S, B, ü, rgi J, Gabay-Maskit S, Maier R, Mastalski T, Yifrach E, Obarska-Kosinska A, Rudowitz M, Erdmann R, Platta HW, Wilmanns M, Schuldiner M, Zalckvar E, Oeljeklaus S, Drepper F, Warscheid B, Phosphorylation of the receptor protein Pex5p modulates import of proteins into peroxisomes. Biol Chem, 404(2-3):135-155(2023) [pubmed]

curator keyword: Biological

submitter keyword: Phosphoproteomics, Peroxisomal Protein Import,Pex5p, Phosphorylation

Bettina Warscheid
contact affiliation	Institute of Biology II, Biochemistry and Functional Proteomics, Signalling Research Centres BIOSS and CIBSS, University of Freiburg, Germany
contact email	bettina.warscheid@biologie.uni-freiburg.de
lab head
Friedel Drepper
contact affiliation	AG Warscheid Biologie II Albert-Ludwigs-Universität Freiburg Schänzlestr. 1 79104 Freiburg Germany
contact email	friedel.drepper@biologie.uni-freiburg.de
dataset submitter

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PRIDE project URI

• PRIDE
  1. PXD015676
     1. Label: PRIDE project
     2. Name: Phosphorylation of the receptor protein Pex5p modulates import of PTS1 cargoes into peroxisomesPhosphorylation of the receptor protein Pex5p modulates import of PTS1 cargoes into peroxisomes