NudC regulated Lis1 stability is essential for the maintenance of dynamic microtubule ends in axon terminals

Dane Kawano, Katherine Pinter, Madison Chlebowski, Ronald S. Petralia, Ya Xian Wang, Alex V. Nechiporuk, Catherine M. Drerup

Research output: Contribution to journalArticlepeer-review

Abstract

In the axon terminal, microtubule stability is decreased relative to the axon shaft. The dynamic microtubule plus ends found in the axon terminal have many functions, including serving as a docking site for the Cytoplasmic dynein motor. Here, we report an unexplored function of dynein in microtubule regulation in axon terminals: regulation of microtubule stability. Using a forward genetic screen, we identified a mutant with an abnormal axon terminal structure owing to a loss of function mutation in NudC. We show that, in the axon terminal, NudC is a chaperone for the protein Lis1. Decreased Lis1 in nudc axon terminals causes dynein/dynactin accumulation and increased microtubule stability. Microtubule dynamics can be restored by pharmacologically inhibiting dynein, implicating excess dynein motor function in microtubule stabilization. Together, our data support a model in which local NudC-Lis1 modulation of the dynein motor is critical for the regulation of microtubule stability in the axon terminal.

Original languageEnglish (US)
Article number105072
JournaliScience
Volume25
Issue number10
DOIs
StatePublished - Oct 21 2022

Keywords

  • Molecular neuroscience
  • developmental neuroscience
  • functional aspects of cell biology

ASJC Scopus subject areas

  • General

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