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Competitive microtubule binding of PEX14 coordinates peroxisomal protein import and motility.
J. Mol. Biol. 433:166765 (2021)
Human PEX14 plays a dual role as docking protein in peroxisomal protein import and as peroxisomal anchor for microtubules (MT), which relates to peroxisome motility. For docking, the conserved N-terminal domain of PEX14 (PEX14-NTD) binds amphipathic alpha-helical ligands, typically comprising one or two aromatic residues, of which human PEX5 possesses eight. Here, we show that the PEX14-NTD also binds to microtubular filaments in vitro with a dissociation constant in nanomolar range. PEX14 interacts with two motifs in the C-terminal region of human ß-tubulin. At least one of the binding motifs is in spatial proximity to the binding site of microtubules (MT) for kinesin. Both PEX14 and kinesin can bind to MT simultaneously. Notably, binding of PEX14 to tubulin can be prevented by its association with PEX5. The data suggest that PEX5 competes peroxisome anchoring to MT by occupying the ß-tubulin-binding site of PEX14. The competitive correlation of matrix protein import and motility may facilitate the homogeneous dispersion of peroxisomes in mammalian cells.
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Publication type
Article: Journal article
Document type
Scientific Article
Keywords
Cytoskeleton ; Pex14 Binding Motifs ; Pex5 Interaction ; Peroxisome Tethering ; Kinesin Motor Domain
ISSN (print) / ISBN
0022-2836
e-ISSN
1089-8638
Journal
Journal of Molecular Biology
Quellenangaben
Volume: 433,
Issue: 5,
Article Number: 166765
Publisher
Elsevier
Publishing Place
24-28 Oval Rd, London Nw1 7dx, England
Non-patent literature
Publications
Reviewing status
Peer reviewed
Institute(s)
Institute of Structural Biology (STB)
Grants
Deutsche Forschungsgemeinschaft