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Gaussmann, S. ; Peschel, R.* ; Ott, J.* ; Zak, K.M. ; Sastre, J.* ; Delhommel, F. ; Popowicz, G.M. ; Boekhoven, J.* ; Schliebs, W.* ; Erdmann, R.* ; Sattler, M.

Modulation of peroxisomal import by the PEX13 SH3 domain and a proximal FxxxF binding motif.

Nat. Commun. 15:3317 (2024)
Publ. Version/Full Text DOI PMC
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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.
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Publication type Article: Journal article
Document type Scientific Article
Corresponding Author
Keywords Membrane-protein Pex13p; Receptor Pex5p Interacts; Saccharomyces-cerevisiae; Evolutionary Conservation; Structural Basis; Biogenesis; Site; Translocation; Recognition; Machinery
ISSN (print) / ISBN 2041-1723
e-ISSN 2041-1723
Journal Nature Communications
Quellenangaben Volume: 15, Issue: 1, Pages: , Article Number: 3317 Supplement: ,
Publisher Nature Publishing Group
Publishing Place London
Non-patent literature Publications
Reviewing status Peer reviewed
Institute(s) Institute of Structural Biology (STB)
Grants EMBO Long-term Fellowship
German Federal Ministry of Research and Education (BMBF) program "Targetvalidierung fur die pharmazeutische Wirkstoffentwicklung"
BMBF VIP+
Deutsche Forschungsgemeinschaft