{"id":{"repo_id":"umn","oai_identifier":"oai:conservancy.umn.edu:11299/215012"},"canonical_url":"https://search.dev.ndltd.org/etd/umn/oai:conservancy.umn.edu:11299/215012","repository":{"repo_id":"umn","name":"University of Minnesota","base_url":"https://conservancy.umn.edu/server/oai/request"},"display":{"title":"Non-Enzymatic Activity Of The Alpha Tubulin Acetyltransferase Alpha-Tat1 Differentially Alters The Stability Of Dynamic And Stable Microtubules","abstract":"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.","abstract_html":"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.","abstract_has_math":false,"creators":["Mannava, Anirudh Gautam"],"institution":null,"degree_name":null,"degree_level":null,"degree_discipline":null,"degree_department":null,"school":null,"contributors":[],"advisors":[],"committee_chairs":[],"committee_members":[],"year":2020,"date_issued":"2020-03","date_published":"2020-03","updated_at":"2026-07-24T05:20:07Z","subjects":["microtubule dynamics","Synaptic bouton","α-tubulin acetyltransferase"],"languages":["en"],"rights":[],"rights_urls":[],"identifier_entries":[]},"links":{"outbound_url":"http://hdl.handle.net/11299/215012","outbound_label":"Handle","outbound_source":"dc:identifier.uri"},"metadata_groups":[{"id":"people","label":"People","entries":[{"key":"dc:creator","label":"Author","values":["Mannava, Anirudh Gautam"]}]},{"id":"academic_context","label":"Academic Context","entries":[{"key":"dc:date.accessioned","label":"Dc Date Accessioned","values":["2020-08-25T13:42:31Z"]},{"key":"dc:date.available","label":"Dc Date Available","values":["2020-08-25T13:42:31Z"]},{"key":"dc:date.issued","label":"Date","values":["2020-03"]},{"key":"dc:type","label":"Dc Type","values":["Thesis or Dissertation"]}]},{"id":"subjects_keywords","label":"Subjects and Keywords","entries":[{"key":"dc:subject","label":"Dc Subject","values":["microtubule dynamics","Synaptic bouton","α-tubulin acetyltransferase"]}]},{"id":"language_rights","label":"Language and Rights","entries":[{"key":"dc:language.iso","label":"Language (ISO)","values":["en"]}]},{"id":"identifiers","label":"Identifiers","entries":[{"key":"dc:identifier.uri","label":"Identifier URI","values":["http://hdl.handle.net/11299/215012"]}]},{"id":"additional","label":"Additional Metadata","entries":[{"key":"dc:description","label":"Description","values":["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."]},{"key":"dc:description.abstract","label":"Abstract","values":["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."]},{"key":"dc:title","label":"Title","values":["Non-Enzymatic Activity Of The Alpha Tubulin Acetyltransferase Alpha-Tat1 Differentially Alters The Stability Of Dynamic And Stable Microtubules"]}]}],"canonical_facts":{"dc:creator":["Mannava, Anirudh Gautam"],"dc:date.accessioned":["2020-08-25T13:42:31Z"],"dc:date.available":["2020-08-25T13:42:31Z"],"dc:date.issued":["2020-03"],"dc:description":["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."],"dc:description.abstract":["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."],"dc:identifier.uri":["http://hdl.handle.net/11299/215012"],"dc:language.iso":["en"],"dc:subject":["microtubule dynamics","Synaptic bouton","α-tubulin acetyltransferase"],"dc:title":["Non-Enzymatic Activity Of The Alpha Tubulin Acetyltransferase Alpha-Tat1 Differentially Alters The Stability Of Dynamic And Stable Microtubules"],"dc:type":["Thesis or Dissertation"]},"updated_at":"2026-07-24T05:20:07Z"}