Acetylated Microtubules Are Preferentially Bundled Leading to Enhanced Kinesin-1 Motility

The motor proteins kinesin and dynein transport organelles, mRNA, proteins, and signaling molecules along the microtubule cytoskeleton. In addition to serving as tracks for transport, the microtubule cytoskeleton directs intracellular trafficking by regulating the activity of motor proteins through...

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Bibliographic Details
Published in:Biophysical journal 2017-10, Vol.113 (7), p.1551-1560
Main Authors: Balabanian, Linda, Berger, Christopher L., Hendricks, Adam G.
Format: Article
Language:English
Subjects:
Acetylation
Animals
Binding sites
Bundling
Cercopithecus aethiops
COS Cells
Cytoskeleton
Dynein
Escherichia coli
Kinesin
Kinesin - metabolism
MicroRNAs
Microtubule-associated proteins
Microtubules - metabolism
Molecular Machines, Motors, and Nanoscale Biophysics
Molecules
mRNA
Organelles
Protein Transport
Proteins
Rats
Recombinant Proteins - metabolism
RNA transport
Signaling
Tau protein
tau Proteins - metabolism
Tubulin
Tubulin - metabolism
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Summary:The motor proteins kinesin and dynein transport organelles, mRNA, proteins, and signaling molecules along the microtubule cytoskeleton. In addition to serving as tracks for transport, the microtubule cytoskeleton directs intracellular trafficking by regulating the activity of motor proteins through the organization of the filament network, microtubule-associated proteins, and tubulin posttranslational modifications. However, it is not well understood how these factors influence motor motility, and in vitro assays and live cell observations often produce disparate results. To systematically examine the factors that contribute to cytoskeleton-based regulation of motor protein motility, we extracted intact microtubule networks from cells and tracked the motility of single fluorescently labeled motor proteins on these cytoskeletons. We find that tubulin acetylation alone does not directly affect kinesin-1 motility. However, acetylated microtubules are predominantly bundled, and bundling enhances kinesin run lengths and provides a greater number of available kinesin binding sites. The neuronal MAP tau is also not sensitive to tubulin acetylation, but enriches preferentially on highly curved regions of microtubules where it strongly inhibits kinesin motility. Taken together, these results suggest that the organization of the microtubule network is a key contributor to the regulation of motor-based transport.
ISSN:0006-3495
1542-0086
DOI:10.1016/j.bpj.2017.08.009