Evidence map›Paper›PMID 29897335›Full record

ArticleeLife2018

Design principles of a microtubule polymerase.

Elisabeth A Geyer, Matthew P Miller, Chad A Brautigam, Sue Biggins, Luke M Rice

Abstract read
In one paragraph

Article in eLife, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.

0numbers the graph read from it
0cells of the map it votes in
33citing papers in PubMed
–field-weighted citation impact
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

33 citing papers in PubMed.

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  13. eLife · 2022
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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

5 authors.

Elisabeth A GeyerDepartments of Biophysics and Biochemistry, UT Southwestern Medical Center, Dallas, United States.
Matthew P MillerHoward Hughes Medical Institute, Division of Basic Sciences, Fred Hutchinson Cancer Research Center, Seattle, United States.ORCID 0000-0003-2012-7546
Chad A BrautigamDepartments of Biophysics and Microbiology, UT Southwestern Medical Center, Dallas, United States.
Sue BigginsHoward Hughes Medical Institute, Division of Basic Sciences, Fred Hutchinson Cancer Research Center, Seattle, United States.ORCID 0000-0002-4499-6319
Luke M RiceDepartments of Biophysics and Biochemistry, UT Southwestern Medical Center, Dallas, United States.ORCID 0000-0001-6551-3307

Funding

Regulation of Chromosome SegregationR01GM064386 · NIGMS · FRED HUTCHINSON CANCER RESEARCH CENTER · PI BIGGINS, SUSAN · 2002 to 2022
$7.2M
CONFORMATION & RECOGNITION IN MICROTUBLE DYNAMICSR01GM098543 · NIGMS · UT SOUTHWESTERN MEDICAL CENTER · PI RICE, LUKE W · 2011 to 2023
$4.2M
Molecular Biophysics Predoctoral Training ProgramT32GM008297 · NIGMS · UT SOUTHWESTERN MEDICAL CENTER · PI CHOOK, YUH MIN · 1989 to 2018
$2.4M
Howard Hughes Medical InstituteNIGMS NIH HHS R01 GM064386NIGMS NIH HHS R01 GM098543NIGMS NIH HHS T32 GM008297
6 · The paper itself

Abstract

Stu2/XMAP215 microtubule polymerases use multiple tubulin-binding TOG domains and a lattice-binding basic region to processively promote faster elongation. How the domain composition and organization of these proteins dictate polymerase activity, end localization, and processivity is unknown. We show that polymerase activity does not require different kinds of TOGs, nor are there strict requirements for how the TOGs are linked. We identify an unexpected antagonism between the tubulin-binding TOGs and the lattice-binding basic region: lattice binding by the basic region is weak when at least two TOGs engage tubulins, strong when TOGs are empty. End-localization of Stu2 requires unpolymerized tubulin, at least two TOGs, and polymerase competence. We propose a 'ratcheting' model for processivity: transfer of tubulin from TOGs to the lattice activates the basic region, retaining the polymerase at the end for subsequent rounds of tubulin binding and incorporation. These results clarify design principles of the polymerase.

Indexed as

Binding SitesCloning, MolecularGene ExpressionGenetic VectorsKineticsMicrotubule-Associated ProteinsMicrotubulesModels, MolecularProtein BindingProtein Conformation, alpha-HelicalProtein Conformation, beta-StrandProtein EngineeringProtein FoldingProtein Interaction Domains and MotifsProtein IsoformsRecombinant ProteinsMicrotubule-Associated ProteinsProtein IsoformsRecombinant ProteinsSaccharomyces cerevisiae ProteinsSTU2 protein, S cerevisiaeTubulincell biologyIn vitro reconstitutionMicrotubule dynamicsMicrotubule polymerasemolecular biophysicsS. cerevisiaestructural biology

Identifiers

PMID29897335
PMCPMC5999394

What OpenQuestion holds

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Registered trials

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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.