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Eur J Cell Biol. 2014 Oct;93(10-12):424-37. doi: 10.1016/j.ejcb.2014.07.006. Epub 2014 Aug 2.

Microtubule acetylation regulates dynamics of KIF1C-powered vesicles and contact of microtubule plus ends with podosomes.

Author information

1
Institut für medizinische Mikrobiologie, Virologie und Hygiene, Universitätsklinikum Eppendorf, Martinistr. 52, 20246 Hamburg, Germany.
2
Institut Curie, Research Center, 75005 Paris, France; Membrane and Cytoskeleton Dynamics, Centre National de la Recherche Scientifique UMR144, 75005 Paris, France.
3
Institut für medizinische Mikrobiologie, Virologie und Hygiene, Universitätsklinikum Eppendorf, Martinistr. 52, 20246 Hamburg, Germany. Electronic address: s.linder@uke.de.

Abstract

Microtubule dynamics are important for a variety of key cellular functions such as intracellular trafficking, adjustment of the cell surface proteome, or adhesion structure turnover. In the current study, we investigate the effects of altered microtubule acetylation levels on the subcellular distribution of kinesins and actin cytoskeletal architecture in primary human macrophages. Microtubule acetylation was altered by overexpression or siRNA-induced depletion of the acetylase MEC-17, or by blocking α-tubulin deacetylation by addition of the inhibitor tubacin. We show that microtubule acetylation influences the subcellular distribution of vesicles associated with the kinesin KIF1C, as well as their directionality, velocity and run length. Moreover, tubulin acetylation alters the targeting frequency of microtubule plus ends on podosomes and influences the number of podosomes per cell and thus the matrix-degrading capacity of macrophages. Collectively, our results point to α-tubulin acetylation as an important modification that impacts on kinesin vesicle dynamics, actin cytoskeletal architecture and cellular function of macrophages.

KEYWORDS:

KIF1C; Kinesin; MEC-17; Macrophage; Microtubule acetylation; Podosomes

PMID:
25151635
DOI:
10.1016/j.ejcb.2014.07.006
[Indexed for MEDLINE]

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