Non-Enzymatic Activity Of The Alpha Tubulin Acetyltransferase Alpha-Tat1 Differentially Alters The Stability Of Dynamic And Stable Microtubules

Neuronal axons terminate as synaptic boutons that form stable yet plastic connections with their targets. Synaptic bouton development relies on an underlying network of both long-lived and dynamic microtubules that provide structural stability for the boutons while also allowing for their growth and remodeling. However, a molecular-scale mechanism that explains how neurons appropriately balance these two microtubule populations remains a mystery. We hypothesized that α-tubulin acetyltransferase (αTAT), which both stabilizes long lived microtubules against mechanical stress via acetylation and has been implicated in promoting microtubule dynamics, could play a role in this process. Biophysical reconstitution experiments revealed that non-enzymatic αTAT1 activity destabilizes dynamic microtubules but does not substantially impact the stability of long-lived microtubules. We propose that the specific suppression of dynamic microtubules by non-enzymatic αTAT activity regulates the remodeling of microtubule networks during synaptic bouton development.

Author dc:creator

• Mannava, Anirudh Gautam

• microtubule dynamics
• Synaptic bouton
• α-tubulin acetyltransferase

Language dc:language.iso

en

Handle dc:identifier.uri

http://hdl.handle.net/11299/215012

OAI identifier oai:identifier

oai:conservancy.umn.edu:11299/215012