{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Fischer S"],"funding":["European Research Council"],"pagination":["135-155"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC9929924"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["404(2-3)"],"pubmed_abstract":["Peroxisomes are organelles with vital functions in metabolism and their dysfunction is associated with human diseases. To fulfill their multiple roles, peroxisomes import 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<sup>2D</sup>) show decreased import of GFP with a PTS1. We show that the binding affinity between a PTS1-protein and Pex5p<sup>2D</sup> is reduced. An <i>in vivo</i> analysis of the effect of the phospho-mimicking mutant on PTS1-proteins revealed that import of most, but not all,"],"journal":["Biological chemistry"],"pubmed_title":["Phosphorylation of the receptor protein Pex5p modulates import of proteins into peroxisomes."],"pmcid":["PMC9929924"],"funding_grant_id":["864068"],"pubmed_authors":["Yifrach E","Fischer S","Wilmanns M","Oeljeklaus S","Maier R","Schuldiner M","Drepper F","Erdmann R","Platta HW","Gabay-Maskit S","Obarska-Kosinska A","Burgi J","Zalckvar E","Rudowitz M","Mastalski T","Warscheid B"],"additional_accession":[]},"is_claimable":false,"name":"Phosphorylation of the receptor protein Pex5p modulates import of proteins into peroxisomes.","description":"Peroxisomes are organelles with vital functions in metabolism and their dysfunction is associated with human diseases. To fulfill their multiple roles, peroxisomes import 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<sup>2D</sup>) show decreased import of GFP with a PTS1. We show that the binding affinity between a PTS1-protein and Pex5p<sup>2D</sup> is reduced. An <i>in vivo</i> analysis of the effect of the phospho-mimicking mutant on PTS1-proteins revealed that import of most, but not all,","dates":{"release":"2023-01-01T00:00:00Z","publication":"2023 Feb","modification":"2026-05-28T11:30:00.142Z","creation":"2025-02-19T03:26:35.523Z"},"accession":"S-EPMC9929924","cross_references":{"pubmed":["36122347"],"doi":["10.1515/hsz-2022-0168"]}}