Evidence map›Paper›PMID 35081332›Full record

ArticleCurrent biology : CB2022

Acetylated α-tubulin K394 regulates microtubule stability to shape the growth of axon terminals.

Harriet A J Saunders, Dena M Johnson-Schlitz, Brian V Jenkins, Peter J Volkert, Sihui Z Yang, Jill Wildonger

Open access · bronzeAbstract read
In one paragraph

Article in Current biology : CB, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.

0numbers the graph read from it
0cells of the map it votes in
30citing papers in PubMed
3.6field-weighted citation impact, top 6% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

30 citing papers in PubMed, 43 citations in OpenAlex.

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  13. A tubulin-MAPKKK pathway engages tubulin isotype interaction for neuroprotection.Proceedings of the National Academy of Sciences of the United States of America · 2025
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4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

6 authors at 1 institution in 1 country.

Harriet A J SaundersIntegrated Program in Biochemistry, University of Wisconsin-Madison, 440 Henry Mall, Madison, WI 53706, USA; Department of Biochemistry, University of Wisconsin-Madison, 440 Henry Mall, Madison, WI 53706, USA.
Dena M Johnson-SchlitzDepartment of Biochemistry, University of Wisconsin-Madison, 440 Henry Mall, Madison, WI 53706, USA.
Brian V JenkinsDepartment of Biochemistry, University of Wisconsin-Madison, 440 Henry Mall, Madison, WI 53706, USA.
Peter J VolkertDepartment of Biochemistry, University of Wisconsin-Madison, 440 Henry Mall, Madison, WI 53706, USA; Biochemistry Scholars Program, University of Wisconsin-Madison, 440 Henry Mall, Madison, WI 53706, USA.
Sihui Z YangDepartment of Biochemistry, University of Wisconsin-Madison, 440 Henry Mall, Madison, WI 53706, USA; Cellular & Molecular Biology Graduate Program, University of Wisconsin-Madison, 1525 Linden Drive, Madison, WI 53706, USA.
Jill WildongerDepartment of Biochemistry, University of Wisconsin-Madison, 440 Henry Mall, Madison, WI 53706, USA. Electronic address: jwildonger@health.ucsd.edu.
University of Wisconsin–Madison · US

Funding

Mechanistic analysis of microtubule dynamics and stability in neuronsR01NS116373 · NINDS · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI WILDONGER, JILL C · 2021 to 2025
$1.7M
NINDS NIH HHS R01 NS116373
6 · The paper itself

Abstract

Microtubules are essential to neuron shape and function. Acetylation of tubulin has the potential to directly tune the behavior and function of microtubules in cells. Although proteomic studies have identified several acetylation sites in α-tubulin, the effects of acetylation at these sites remains largely unknown. This includes the highly conserved residue lysine 394 (K394), which is located at the αβ-tubulin dimer interface. Using a fly model, we show that α-tubulin K394 is acetylated in the nervous system and is an essential residue. We found that an acetylation-blocking mutation in endogenous α-tubulin, K394R, perturbs the synaptic morphogenesis of motoneurons and reduces microtubule stability. Intriguingly, the K394R mutation has opposite effects on the growth of two functionally and morphologically distinct motoneurons, revealing neuron-type-specific responses when microtubule stability is altered. Eliminating the deacetylase HDAC6 increases K394 acetylation, and the over-expression of HDAC6 reduces microtubule stability similar to the K394R mutant. Thus, our findings implicate α-tubulin K394 and its acetylation in the regulation of microtubule stability and suggest that HDAC6 regulates K394 acetylation during synaptic morphogenesis.

Indexed as

Presynaptic TerminalsTubulinAcetylationHistone Deacetylase 6Histone DeacetylasesMicrotubulesProteomicsHistone Deacetylase 6Histone DeacetylasesTubulinacetylationcytoskeletonDrosophilamicrotubuleneuronsynaptic morphogenesis

Identifiers

PMID35081332
PMCPMC8843987
OpenAlexW4206996219

What OpenQuestion holds

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Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.