Phosphorylation of the receptor protein Pex5p modulates import of proteins into peroxisomes

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 (Pex5p2D) show decreased import of GFP with a PTS1. We show that the binding affinity between a PTS1-protein and Pex5p2D is reduced. An in vivo analysis of the effect of the phospho-mimicking mutant on PTS1-proteins revealed that import of most, but not all, cargos is affected. The physiological effect of the phosphomimetic mutations correlates 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. In a broader view, this suggests that posttranslational modifications can function in fine-tuning the peroxisomal protein composition and, thus, cellular metabolism

Angaben zum Objekt

• Standort: Deutsche Nationalbibliothek Frankfurt am Main
• Umfang: Online-Ressource
• Sprache: Englisch
• Anmerkungen: Biological chemistry. - 404, 2-3 (2023) , 135-155, ISSN: 1437-4315

Beteiligte, Orts- und Zeitangaben

• Ereignis: Veröffentlichung
• (wo): Freiburg
• (wer): Universität
• (wann): 2023
• Urheber: Fischer, Sven ; Bürgi, Jérôme ; Gabay-Maskit, Shiran ; Maier, Renate ; Mastalski, Thomas ; Yifrach, Eden ; Obarska-Kosinska, Agnieszka ; Rudowitz, Markus ; Erdmann, Ralf ; Platta, Harald W. ; Wilmanns, Matthias ; Schuldiner, Maya ; Zalckvar, Einat ; Oeljeklaus, Silke ; Drepper, Friedel ; Warscheid, Bettina

Weitere Informationen

• DOI: 10.1515/hsz-2022-0168
• URN: urn:nbn:de:bsz:25-freidok-2337829
• Rechteinformation: Open Access; Der Zugriff auf das Objekt ist unbeschränkt möglich.
• Letzte Aktualisierung: 25.03.2025, 13:48 MEZ