Evidence map›Paper›PMID 37093124›Full record

ArticleThe Journal of cell biology2023

The motor domain of the kinesin Kip2 promotes microtubule polymerization at microtubule tips.

Xiuzhen Chen, Didier Portran, Lukas A Widmer, Marcel M Stangier, Mateusz P Czub, Dimitris Liakopoulos, Jörg Stelling, Michel O Steinmetz, Yves Barral

Open access · hybridAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in The Journal of cell biology, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing papers in PubMed
1.7field-weighted citation impact, top 18% 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

3 citing papers in PubMed, 8 citations in OpenAlex.

  1. Article
  2. Article
  3. TOR Complex 1: Orchestrating Nutrient Signaling and Cell Cycle Progression.International journal of molecular sciences · 2023
    Review
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

9 authors at 5 institutions in 3 countries.

Xiuzhen ChenInstitute of Biochemistry, Eidgenössische Technische Hochschule Zürich , Zurich, Switzerland.ORCID 0000-0002-3027-6441
Didier Portran *CRBM, Université de Montpellier , CNRS, Montpellier, France.ORCID 0000-0002-0356-398X
Lukas A Widmer *Department of Biosystems Science and Engineering, Eidgenössische Technische Hochschule Zürich, and Swiss Institute of Bioinformatics, Basel, Switzerland.ORCID 0000-0003-1471-3493
Marcel M Stangier *Department of Biology and Chemistry, Laboratory of Biomolecular Research, Paul Scherrer Institute, Villigen, Switzerland.ORCID 0000-0001-6837-0823
Mateusz P CzubDepartment of Biology and Chemistry, Laboratory of Biomolecular Research, Paul Scherrer Institute, Villigen, Switzerland.ORCID 0000-0001-8973-4569
Dimitris LiakopoulosCRBM, Université de Montpellier , CNRS, Montpellier, France.ORCID 0000-0001-6089-8877
Jörg StellingDepartment of Biosystems Science and Engineering, Eidgenössische Technische Hochschule Zürich, and Swiss Institute of Bioinformatics, Basel, Switzerland.ORCID 0000-0002-1145-891X
Michel O SteinmetzDepartment of Biology and Chemistry, Laboratory of Biomolecular Research, Paul Scherrer Institute, Villigen, Switzerland.ORCID 0000-0001-6157-3687
Yves BarralInstitute of Biochemistry, Eidgenössische Technische Hochschule Zürich , Zurich, Switzerland.ORCID 0000-0002-0989-3373
Board of the Swiss Federal Institutes of Technology · CHCentre National de la Recherche Scientifique · FRPaul Scherrer Institute · CHSIB Swiss Institute of Bioinformatics · CHUniversity of Basel · CH

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Kinesins are microtubule-dependent motor proteins, some of which moonlight as microtubule polymerases, such as the yeast protein Kip2. Here, we show that the CLIP-170 ortholog Bik1 stabilizes Kip2 at microtubule ends where the motor domain of Kip2 promotes microtubule polymerization. Live-cell imaging and mathematical estimation of Kip2 dynamics reveal that disrupting the Kip2-Bik1 interaction aborts Kip2 dwelling at microtubule ends and abrogates its microtubule polymerization activity. Structural modeling and biochemical experiments identify a patch of positively charged residues that enables the motor domain to bind free tubulin dimers alternatively to the microtubule shaft. Neutralizing this patch abolished the ability of Kip2 to promote microtubule growth both in vivo and in vitro without affecting its ability to walk along microtubules. Our studies suggest that Kip2 utilizes Bik1 as a cofactor to track microtubule tips, where its motor domain then recruits free tubulin and catalyzes microtubule assembly.

Indexed as

KinesinsMicrotubule-Associated ProteinsMolecular Motor ProteinsSaccharomyces cerevisiae ProteinsTubulinMicrotubulesPolymerizationSaccharomyces cerevisiaeBik1 protein, S cerevisiaeKinesinsKIP2 protein, S cerevisiaeMicrotubule-Associated ProteinsMolecular Motor ProteinsSaccharomyces cerevisiae ProteinsTubulin

Identifiers

PMID37093124
PMCPMC10130750
OpenAlexW4366821702

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.