PuSH - Publikationsserver des Helmholtz Zentrums München

Reuter, M.* ; Kooshapur, H. ; Suda, J.G.* ; Gaussmann, S. ; Neuhaus, A.* ; Brühl, L.* ; Bharti, P.* ; Jung, M.* ; Schliebs, W.* ; Sattler, M. ; Erdmann, R.*

Competitive microtubule binding of PEX14 coordinates peroxisomal protein import and motility.

J. Mol. Biol. 433:166765 (2021)
DOI Verlagsversion bestellen
Open Access Green: Postprint online verfügbar 03/2022
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.
Altmetric
Weitere Metriken?
Zusatzinfos bearbeiten [➜Einloggen]
Publikationstyp Artikel: Journalartikel
Dokumenttyp Wissenschaftlicher Artikel
Schlagwörter Cytoskeleton ; Pex14 Binding Motifs ; Pex5 Interaction ; Peroxisome Tethering ; Kinesin Motor Domain
ISSN (print) / ISBN 0022-2836
e-ISSN 1089-8638
Quellenangaben Band: 433, Heft: 5, Seiten: , Artikelnummer: 166765 Supplement: ,
Verlag Elsevier
Verlagsort 24-28 Oval Rd, London Nw1 7dx, England
Begutachtungsstatus Peer reviewed
Förderungen Deutsche Forschungsgemeinschaft