Evidence map›Paper›PMID 26875866›Full record

ArticleCell2016

Graded Control of Microtubule Severing by Tubulin Glutamylation.

Max L Valenstein, Antonina Roll-Mecak

Open access · bronzeAbstract read
In one paragraph

Article in Cell, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 161 papers.

0numbers the graph read from it
0cells of the map it votes in
161citing papers in PubMed
17.2field-weighted citation impact, top 1% 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

161 citing papers in PubMed, 266 citations in OpenAlex.

  1. Review
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  14. An Orthogonal Way of Writing the Tubulin Code.Cytoskeleton (Hoboken, N.J.) · 2026
    Review
  15. Article
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101 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

2 authors at 1 institution in 1 country.

Max L ValensteinCell Biology and Biophysics Unit, Porter Neuroscience Research Center, National Institute of Neurological Disorders and Stroke, Bethesda, MD 20892, USA.
Antonina Roll-MecakCell Biology and Biophysics Unit, Porter Neuroscience Research Center, National Institute of Neurological Disorders and Stroke, Bethesda, MD 20892, USA; National Heart, Lung and Blood Institute, Bethesda, MD 20892, USA. Electronic address: antonina@mail.nih.gov.
National Institute of Neurological Disorders and Stroke · US

Funding

Readout of the tubulin code by cellular effectorsZIANS003164 · NINDS · NATIONAL INSTITUTE OF NEUROLOGICAL DISORDERS AND STROKE · PI ROLL-MECAK, ANTONINA · 2017 to 2025
$11.7M
Mechanisms of molecular machines that regulate the neuronal cytoskeletonZIANS003122 · NINDS · NATIONAL INSTITUTE OF NEUROLOGICAL DISORDERS AND STROKE · PI ROLL-MECAK, ANTONINA · 2010 to 2016
$9.9M
Mechanism of microtubule severing enzymesZIANS003165 · NINDS · NATIONAL INSTITUTE OF NEUROLOGICAL DISORDERS AND STROKE · PI ROLL-MECAK, ANTONINA · 2017 to 2025
$9.2M
Intramural NIH HHS ZIA NS003122
6 · The paper itself

Abstract

Microtubule-severing enzymes are critical for the biogenesis and maintenance of complex microtubule arrays in axons, spindles, and cilia where tubulin detyrosination, acetylation, and glutamylation are abundant. These modifications exhibit stereotyped patterns suggesting spatial and temporal control of microtubule functions. Using human-engineered and differentially modified microtubules we find that glutamylation is the main regulator of the hereditary spastic paraplegia microtubule severing enzyme spastin. Glutamylation acts as a rheostat and tunes microtubule severing as a function of glutamate number added per tubulin. Unexpectedly, glutamylation is a non-linear biphasic tuner and becomes inhibitory beyond a threshold. Furthermore, the inhibitory effect of localized glutamylation propagates across neighboring microtubules, modulating severing in trans. Our work provides the first quantitative evidence for a graded response to a tubulin posttranslational modification and a biochemical link between tubulin glutamylation and complex architectures of microtubule arrays such as those in neurons where spastin deficiency causes disease.

Indexed as

Protein Processing, Post-TranslationalAdenosine TriphosphatasesBiomechanical PhenomenaGlutamic AcidHumansMicrotubulesNeuronsProtein EngineeringSpastic Paraplegia, HereditarySpastinTubulinAdenosine TriphosphatasesGlutamic AcidSpastinSPAST protein, humanTubulin

Identifiers

PMID26875866
PMCPMC6459029
OpenAlexW2269299490

What OpenQuestion holds

Textmetadata
LicenceTDM
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.