Evidence map›Paper›PMID 28783150›Full record

ArticleNature structural & molecular biology2017

Katanin spiral and ring structures shed light on power stroke for microtubule severing.

Elena Zehr, Agnieszka Szyk, Grzegorz Piszczek, Ewa Szczesna, Xiaobing Zuo, Antonina Roll-Mecak

Open access · greenAbstract read
In one paragraph

Article in Nature structural & molecular biology, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 61 papers.

0numbers the graph read from it
0cells of the map it votes in
61citing papers in PubMed
6.7field-weighted citation impact, top 2% 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

61 citing papers in PubMed, 113 citations in OpenAlex.

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1 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

6 authors at 3 institutions in 1 country.

Elena ZehrCell Biology and Biophysics Unit, Porter Neuroscience Research Center, National Institute of Neurological Disorders and Stroke, Bethesda, Maryland, USA.
Agnieszka SzykCell Biology and Biophysics Unit, Porter Neuroscience Research Center, National Institute of Neurological Disorders and Stroke, Bethesda, Maryland, USA.
Grzegorz PiszczekBiophysics Core, National Heart, Lung and Blood Institute, Bethesda, Maryland, USA.
Ewa SzczesnaCell Biology and Biophysics Unit, Porter Neuroscience Research Center, National Institute of Neurological Disorders and Stroke, Bethesda, Maryland, USA.
Xiaobing ZuoX-ray Science Division, Advanced Photon Source, Argonne National Laboratory, Argonne, Illinois, USA.
Antonina Roll-MecakCell Biology and Biophysics Unit, Porter Neuroscience Research Center, National Institute of Neurological Disorders and Stroke, Bethesda, Maryland, USA.ORCID http://orcid.org/0000-0003-2621-7307
National Institute of Neurological Disorders and Stroke · USNational Heart Lung and Blood Institute · USArgonne National Laboratory · US

Funding

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 NS003122Intramural NIH HHS ZIA NS003165
6 · The paper itself

Abstract

Microtubule-severing enzymes katanin, spastin and fidgetin are AAA ATPases important for the biogenesis and maintenance of complex microtubule arrays in axons, spindles and cilia. Because of a lack of known 3D structures for these enzymes, their mechanism of action has remained poorly understood. Here we report the X-ray crystal structure of the monomeric AAA katanin module from Caenorhabditis elegans and cryo-EM reconstructions of the hexamer in two conformations. The structures reveal an unexpected asymmetric arrangement of the AAA domains mediated by structural elements unique to microtubule-severing enzymes and critical for their function. The reconstructions show that katanin cycles between open spiral and closed ring conformations, depending on the ATP occupancy of a gating protomer that tenses or relaxes interprotomer interfaces. Cycling of the hexamer between these conformations would provide the power stroke for microtubule severing.

Indexed as

Adenosine TriphosphatasesAdenosine TriphosphateAnimalsCaenorhabditis elegansCryoelectron MicroscopyCrystallography, X-RayKataninModels, MolecularProtein BindingProtein ConformationAdenosine TriphosphatasesAdenosine TriphosphateKatanin

Identifiers

PMID28783150
PMCPMC7152510
OpenAlexW2745147988

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.