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Mol Biol Cell. 2017 Sep 1;28(18):2400-2409. doi: 10.1091/mbc.E16-11-0756. Epub 2017 Jul 12.

CENP-F couples cargo to growing and shortening microtubule ends.

Author information

1
Institute of Biochemistry, ETH Zurich, ZH 8093 Zurich, Switzerland.
2
Department of Bioengineering and Bioinformatics, Moscow State University, 119991 Moscow, Russia.
3
Center for Theoretical Problems of Physicochemical Pharmacology, Russian Academy of Sciences, 119991 Moscow, Russia.
4
Center for Theoretical Problems of Physicochemical Pharmacology, Russian Academy of Sciences, 119991 Moscow, Russia benoit.kornmann@bc.biol.ethz.ch v.volkov@tudelft.nl.
5
Institute of Biochemistry, ETH Zurich, ZH 8093 Zurich, Switzerland benoit.kornmann@bc.biol.ethz.ch v.volkov@tudelft.nl.

Abstract

Dynamic microtubule ends exert pulling and pushing forces on intracellular membranes and organelles. However, the mechanical linkage of microtubule tips to their cargoes is poorly understood. CENP-F is a nonmotor microtubule-binding protein that participates in microtubule binding at kinetochores and in the mitotic redistribution of the mitochondrial network. CENP-F-driven mitochondrial transport is linked to growing microtubule tips, but the underlying molecular mechanisms are unknown. Here we show that CENP-F tracks growing microtubule ends in living cells. In vitro reconstitution demonstrates that microtubule tips can transport mitochondria and CENP-F-coated artificial cargoes over micrometer-long distances during both growing and shrinking phases. Based on these and previous observations, we suggest that CENP-F might act as a transporter of mitochondria and other cellular cargoes by attaching them to dynamic microtubule ends during both polymerization and depolymerization of tubulin.

PMID:
28701340
PMCID:
PMC5576903
DOI:
10.1091/mbc.E16-11-0756
[Indexed for MEDLINE]
Free PMC Article

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