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EMBO J. 2016 Jun 1;35(11):1175-85. doi: 10.15252/embj.201593071. Epub 2016 Mar 11.

Tyrosination of α-tubulin controls the initiation of processive dynein-dynactin motility.

Author information

1
Department of Cellular and Molecular Pharmacology, the Howard Hughes Medical Institute University of California, San Francisco, CA, USA.
2
Department of Cellular and Molecular Pharmacology, the Howard Hughes Medical Institute University of California, San Francisco, CA, USA minhaj@instem.res.in.

Abstract

Post-translational modifications (PTMs) of α/β-tubulin are believed to regulate interactions with microtubule-binding proteins. A well-characterized PTM involves in the removal and re-ligation of the C-terminal tyrosine on α-tubulin, but the purpose of this tyrosination-detyrosination cycle remains elusive. Here, we examined the processive motility of mammalian dynein complexed with dynactin and BicD2 (DDB) on tyrosinated versus detyrosinated microtubules. Motility was decreased ~fourfold on detyrosinated microtubules, constituting the largest effect of a tubulin PTM on motor function observed to date. This preference is mediated by dynactin's microtubule-binding p150 subunit rather than dynein itself. Interestingly, on a bipartite microtubule consisting of tyrosinated and detyrosinated segments, DDB molecules that initiated movement on tyrosinated tubulin continued moving into the segment composed of detyrosinated tubulin. This result indicates that the α-tubulin tyrosine facilitates initial motor-tubulin encounters, but is not needed for subsequent motility. Our results reveal a strong effect of the C-terminal α-tubulin tyrosine on dynein-dynactin motility and suggest that the tubulin tyrosination cycle could modulate the initiation of dynein-driven motility in cells.

KEYWORDS:

dynein; microtubule; post‐translational modification; tyrosination

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PMID:
26968983
PMCID:
PMC4888239
DOI:
10.15252/embj.201593071
[Indexed for MEDLINE]
Free PMC Article

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