Microtubule acetylation is required for mechanosensation in Drosophila
نویسندگان
چکیده
At the cellular level, α-tubulin acetylation alters the structure of microtubules to render them mechanically resistant to compressive forces. How this biochemical property of microtubule acetylation relates to mechanosensation remains unknown, though prior studies have shown that microtubule acetylation plays a role in touch perception. Here, we identify the major Drosophila α-tubulin acetylase (dTAT) and show that it plays key roles in several forms of mechanosensation while exerting little effect on other sensory modalities. dTAT is highly expressed in neurons of the larval peripheral nervous system (PNS), but is not required for normal neuronal morphogenesis. We show that mutation of the acetylase gene or the K40 acetylation site in α-tubulin impairs mechanical sensitivity in sensory neurons and behavioral responses to gentle touch, harsh touch, gravity, and sound stimulus, but not thermal stimulus. Finally, we show that dTAT is required for mechanically-induced activation of NOMPC, a microtubule-associated transient receptor potential channel, and functions to maintain integrity of the microtubule cytoskeleton in response to mechanical stimulation. peer-reviewed) is the author/funder. All rights reserved. No reuse allowed without permission. The copyright holder for this preprint (which was not . http://dx.doi.org/10.1101/252601 doi: bioRxiv preprint first posted online Jan. 23, 2018;
منابع مشابه
A doublecortin containing microtubule-associated protein is implicated in mechanotransduction in Drosophila sensory cilia
Mechanoreceptors are sensory cells that transduce mechanical stimuli into electrical signals and mediate the perception of sound, touch and acceleration. Ciliated mechanoreceptors possess an elaborate microtubule cytoskeleton that facilitates the coupling of external forces to the transduction apparatus. In a screen for genes preferentially expressed in Drosophila campaniform mechanoreceptors, ...
متن کاملRab11 is required for maintenance of cell shape via βPS integrin mediated cell adhesion in Drosophila
In eukaryotes, vesicle trafficking is regulated by the small monomeric GTPases of the Rab protein family. Rab11, (a subfamily of the Ypt/Rab gene family) an evolutionarily conserved, ubiquitously expressed subfamily of small monomeric Rab GTPases, has been implicated in regulating vesicular trafficking through the recycling of endosomal compartment. In an earlier communication, we have shown th...
متن کاملO-12: Tubulin Reversible Acetylation – Driving The Moves and The Moves Behind The Drive
Background Asthenozoospermia accounts for almost 50% of the cases of male infertility. Our study investigating phosphoproteins differentially expressed in asthenozoosperm has identified the phosphoproteins relevant to sperm motility and the signature molecules likely to be altered in asthenozoospermia. The 66 phosphoproteins differentially expressed included four alpha tubulin isoforms which we...
متن کاملI-16: Tubulin Reversible Acetylation – Driving The Moves and The Moves Behind The Drive
Background Asthenozoospermia accounts for almost 50% of the cases of male infertility. Our study investigating phosphoproteins differentially expressed in asthenozoosperm has identified the phosphoproteins relevant to sperm motility and the signature molecules likely to be altered in asthenozoospermia. The 66 phosphoproteins differentially expressed included four alpha tubulin isoforms which we...
متن کاملEffects of mutating α-tubulin lysine 40 on sensory dendrite development
Microtubules are essential for neuronal structure and function. Axonal and dendritic microtubules are enriched in post-translational modifications that impact microtubule dynamics, transport and microtubule-associated proteins. Acetylation of α-tubulin lysine 40 (K40) is a prominent and conserved modification of neuronal microtubules. However, the cellular role of microtubule acetylation remain...
متن کامل