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Prion protein impairs kinesin-driven transport

Authors
Publisher
Elsevier Inc.
Publication Date
Volume
425
Issue
4
Identifiers
DOI: 10.1016/j.bbrc.2012.07.153
Keywords
  • Prion Protein
  • Microtubule
  • Prion Disease
  • Kinesin
  • Division Spindle
Disciplines
  • Biology

Abstract

Abstract Our previous studies have demonstrated that prion protein (PrP) leads to disassembly of microtubular cytoskeleton through binding to tubulin and its oligomerization. Here we found that PrP-treated cells exhibited improper morphology of mitotic spindles. Formation of aberrant spindles may result not only from altered microtubule dynamics – as expected from PrP-induced tubulin oligomerization – but also from impairing the function of molecular motors. Therefore we checked whether binding of PrP to microtubules affected movement generated by Ncd – a kinesin responsible for the proper organization of division spindles. We found that PrP inhibited Ncd-driven transport of microtubules. Most probably, the inhibition of the microtubule movement resulted from PrP-induced changes in the microtubule structure since Ncd-microtubule binding was reduced already at low PrP to tubulin molar ratios. This study suggests another plausible mechanism of PrP cytotoxicity related to the interaction with tubulin, namely impeding microtubule-dependent transport.

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