期刊
SCIENCE ADVANCES
卷 5, 期 12, 页码 -出版社
AMER ASSOC ADVANCEMENT SCIENCE
DOI: 10.1126/sciadv.aax2705
关键词
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资金
- EMBO Short-Term Fellowships [ASTF 174-2016]
- TAU Global Research and Training Fellowship
- Ela Kodesz Institute
- Scientific and Academic Cooperation Office of the French embassy in Tel Aviv
- Israel Science Foundation [1688/16]
- FRM [ALTF 693-2015]
- EMBO LTF [ALTF 693-2015]
- FRS-FNRS
- Fonds Leon Fredericq
- Fondation Medicale Reine Elisabeth
- Fondation Simone et Pierre Clerdent
- Belgian Science Policy [IAP-VII network] [P7/20, P7/10]
- ERANET Neuron STEM-MCD
- NeuroTalk
- Agence Nationale de la Recherche [ANR-14-CE35-0027-01 PASSAGE, ANR-15-JPWG-0003-05 JPND CIRCPROT, ANR-15-IDEX-02 NeuroCoG, ANR-10-IDEX-0001-02, ANR-11-LBX-003]
- LABEX celtisphybio 8
- Fondation pour la Recherche Medicale (FRM, equipe labellisee)
- Institut Curie
- French National Research Agency (ANR) [ANR-17-CE13-0021]
- Fondation pour la Recherche Medicale (FRM) [DEQ20170336756]
- European Union [675737]
- FRM grant [FDT201904008210]
- Fondation Vaincre Alzheimer [FR-16055p]
Microtubules are polymerized dimers of alpha- and beta-tubulin that underlie a broad range of cellular activities. Acetylation of alpha-tubulin by the acetyltransferase ATAT1 modulates microtubule dynamics and functions in neurons. However, it remains unclear how this enzyme acetylates microtubules over long distances in axons. Here, we show that loss of ATAT1 impairs axonal transport in neurons in vivo, and cell-free motility assays confirm a requirement of alpha-tubulin acetylation for proper bidirectional vesicular transport. Moreover, we demonstrate that the main cellular pool of ATAT1 is transported at the cytosolic side of neuronal vesicles that are moving along axons. Together, our data suggest that axonal transport of ATAT1-enriched vesicles is the predominant driver of alpha-tubulin acetylation in axons.
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