Sep 25, 2015

Tyrosination of α-Tubulin Controls The Initiation of Processive Dynein-Dynactin Motility

BioRxiv : the Preprint Server for Biology
Richard J McKenneyMinhaj Sirajuddin


Post-translational modifications (PTMs) of αβtubulin are believed to regulate interactions with microtubule binding proteins. A well-characterized PTM involves 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 ~4-fold 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 chimeric microtubules, DDB molecules that initiated movement on tyrosinated tubulin continued moving into a region 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.

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Mentioned in this Paper

DCTN4 protein, human
Dynein Activity
Carboxy-Terminal Amino Acid
Light-driven Proton Transport
Cell Motility
Post-Translational Protein Processing
DDB Chlorinated Hydrocarbons
Tubulin-tyrosine Ligase Activity
Chimera Organism
Transcription Initiation

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