Tyrosination of alpha-tubulin controls the initiation of processive dynein-dynactin motility.
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McKenney RJ, Huynh W, Vale RD, Sirajuddin M
Tyrosination of alpha-tubulin controls the initiation of processive dynein-dynactin motility.
EMBO J. 2016 Jun 1;35(11):1175-85. doi: 10.15252/embj.201593071. Epub 2016 Mar 11.
- PubMed ID
- 26968983 [ View in PubMed]
- Abstract
Post-translational modifications (PTMs) of alpha/beta-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 alpha-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 alpha-tubulin tyrosine facilitates initial motor-tubulin encounters, but is not needed for subsequent motility. Our results reveal a strong effect of the C-terminal alpha-tubulin tyrosine on dynein-dynactin motility and suggest that the tubulin tyrosination cycle could modulate the initiation of dynein-driven motility in cells.