Modulation of peroxisomal import by the PEX13 SH3 domain and a proximal FxxxF binding motif.
Journal
Nature communications
ISSN: 2041-1723
Titre abrégé: Nat Commun
Pays: England
ID NLM: 101528555
Informations de publication
Date de publication:
18 Apr 2024
18 Apr 2024
Historique:
received:
05
01
2023
accepted:
08
04
2024
medline:
19
4
2024
pubmed:
18
4
2024
entrez:
17
4
2024
Statut:
epublish
Résumé
Import of proteins into peroxisomes depends on PEX5, PEX13 and PEX14. By combining biochemical methods and structural biology, we show that the C-terminal SH3 domain of PEX13 mediates intramolecular interactions with a proximal FxxxF motif. The SH3 domain also binds WxxxF peptide motifs in the import receptor PEX5, demonstrating evolutionary conservation of such interactions from yeast to human. Strikingly, intramolecular interaction of the PEX13 FxxxF motif regulates binding of PEX5 WxxxF/Y motifs to the PEX13 SH3 domain. Crystal structures reveal how FxxxF and WxxxF/Y motifs are recognized by a non-canonical surface on the SH3 domain. The PEX13 FxxxF motif also mediates binding to PEX14. Surprisingly, the potential PxxP binding surface of the SH3 domain does not recognize PEX14 PxxP motifs, distinct from its yeast ortholog. Our data show that the dynamic network of PEX13 interactions with PEX5 and PEX14, mediated by diaromatic peptide motifs, modulates peroxisomal matrix import.
Identifiants
pubmed: 38632234
doi: 10.1038/s41467-024-47605-w
pii: 10.1038/s41467-024-47605-w
pmc: PMC11024197
doi:
Substances chimiques
Membrane Proteins
0
Peroxisome-Targeting Signal 1 Receptor
0
Peptides
0
PEX13 protein, human
0
PEX13 protein, S cerevisiae
0
Saccharomyces cerevisiae Proteins
0
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Pagination
3317Subventions
Organisme : Deutsche Forschungsgemeinschaft (German Research Foundation)
ID : FOR905 project number 219314758
Informations de copyright
© 2024. The Author(s).
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