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

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

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2020-03

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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.

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University of Minnesota M.S. thesis. March 2020. Major: Molecular, Cellular, Developmental Biology and Genetics. Advisor: Melissa Gardner. 1 computer file (PDF); 26 pages + 3 supplementary files.

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Mannava, Anirudh Gautam. (2020). Non-Enzymatic Activity Of The Alpha Tubulin Acetyltransferase Alpha-Tat1 Differentially Alters The Stability Of Dynamic And Stable Microtubules. Retrieved from the University Digital Conservancy, https://hdl.handle.net/11299/215012.

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