Evidence map›Paper›PMID 28697331›Full record

ArticleDevelopmental cell2017

A Tubulin Binding Switch Underlies Kip3/Kinesin-8 Depolymerase Activity.

Hugo Arellano-Santoyo, Elisabeth A Geyer, Ema Stokasimov, Geng-Yuan Chen, Xiaolei Su, William Hancock, Luke M Rice, David Pellman

Open access · bronzeAbstract read
In one paragraph

Article in Developmental cell, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 41 papers.

0numbers the graph read from it
0cells of the map it votes in
41citing papers in PubMed
4.8field-weighted citation impact, top 4% 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

41 citing papers in PubMed, 80 citations in OpenAlex.

  1. Article
  2. Article
  3. Mechanism and regulation of kinesin motors.Nature reviews. Molecular cell biology · 2025
    Review
  4. Review
  5. Modeling study of kinesin-13 MCAK microtubule depolymerase.European biophysics journal : EBJ · 2024
    Article
  6. Article
  7. Article
  8. Review
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Atomic force microscopy reveals distinct protofilament-scale structural dynamics in depolymerizing microtubule arrays.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  17. Review
  18. Review
  19. Article
  20. Article
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

8 authors at 6 institutions in 1 country.

Hugo Arellano-SantoyoHoward Hughes Medical Institute, Chevy Chase, MD 20815, USA; Department of Pediatric Oncology, Dana-Farber Cancer Institute, Boston, MA 02215, USA; Department of Cell Biology, Harvard Medical School, Boston, MA 02215, USA.
Elisabeth A GeyerDepartment of Biophysics, UT Southwestern, Dallas, TX 75390, USA.
Ema StokasimovHoward Hughes Medical Institute, Chevy Chase, MD 20815, USA; Department of Pediatric Oncology, Dana-Farber Cancer Institute, Boston, MA 02215, USA; Department of Cell Biology, Harvard Medical School, Boston, MA 02215, USA.
Geng-Yuan ChenDepartment of Biomedical Engineering, Penn State University, University Park, PA 16802, USA.
Xiaolei SuDepartment of Cellular and Molecular Pharmacology, University of California San Francisco, San Francisco, CA 94143, USA.
William HancockDepartment of Biomedical Engineering, Penn State University, University Park, PA 16802, USA.
Luke M RiceDepartment of Biophysics, UT Southwestern, Dallas, TX 75390, USA.
David PellmanHoward Hughes Medical Institute, Chevy Chase, MD 20815, USA; Department of Pediatric Oncology, Dana-Farber Cancer Institute, Boston, MA 02215, USA; Department of Cell Biology, Harvard Medical School, Boston, MA 02215, USA. Electronic address: david_pellman@dfci.harvard.edu.
Pennsylvania State University · USThe University of Texas Southwestern Medical Center · USDana-Farber Cancer Institute · USHarvard University · USHoward Hughes Medical Institute · USUniversity of California, San Francisco · US

Funding

CONFORMATION & RECOGNITION IN MICROTUBLE DYNAMICSR01GM098543 · NIGMS · UT SOUTHWESTERN MEDICAL CENTER · PI RICE, LUKE W · 2011 to 2023
$4.2M
CELL POLARITY AND SPINDLE POSITIONR01GM061345 · NIGMS · DANA-FARBER CANCER INSTITUTE · PI PELLMAN, DAVID S · 2000 to 2011
$3.6M
Polyploidy, Aneuploidy and Genome StabilityR01CA213404 · NCI · DANA-FARBER CANCER INST · PI PELLMAN, DAVID S · 2017 to 2024
$3.5M
Molecular mechanism of kinesin motilityR01GM076476 · NIGMS · PENNSYLVANIA STATE UNIVERSITY, THE · PI HANCOCK, WILLIAM OLAF · 2006 to 2019
$3.5M
Cell Cycle Control of the CytoskeletonR37GM061345 · NIGMS · DANA-FARBER CANCER INST · PI PELLMAN, DAVID S · 2014 to 2023
$3.4M
Molecular Biophysics Predoctoral Training ProgramT32GM008297 · NIGMS · UT SOUTHWESTERN MEDICAL CENTER · PI CHOOK, YUH MIN · 1989 to 2018
$2.4M
Howard Hughes Medical InstituteNCI NIH HHS R01 CA213404NIGMS NIH HHS R01 GM061345NIGMS NIH HHS R01 GM076476NIGMS NIH HHS R01 GM098543NIGMS NIH HHS R37 GM061345NIGMS NIH HHS T32 GM008297
6 · The paper itself

Abstract

Kinesin-8 motors regulate the size of microtubule structures, using length-dependent accumulation at the plus end to preferentially disassemble long microtubules. Despite extensive study, the kinesin-8 depolymerase mechanism remains under debate. Here, we provide evidence for an alternative, tubulin curvature-sensing model of microtubule depolymerization by the budding yeast kinesin-8, Kip3. Kinesin-8/Kip3 uses ATP hydrolysis, like other kinesins, for stepping on the microtubule lattice, but at the plus end Kip3 undergoes a switch: its ATPase activity is suppressed when it binds tightly to the curved conformation of tubulin. This prolongs plus-end binding, stabilizes protofilament curvature, and ultimately promotes microtubule disassembly. The tubulin curvature-sensing model is supported by our identification of Kip3 structural elements necessary and sufficient for plus-end binding and depolymerase activity, as well as by the identification of an α-tubulin residue specifically required for the Kip3-curved tubulin interaction. Together, these findings elucidate a major regulatory mechanism controlling the size of cellular microtubule structures.

Indexed as

Adenosine TriphosphateAnimalsBiocatalysisHydrolysisKinesinsMicrotubulesModels, BiologicalModels, MolecularMutant ProteinsPolymerizationProtein BindingProtein Structure, SecondarySaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSus scrofaTubulinAdenosine TriphosphateKinesinsKIP3 protein, S cerevisiaeMutant ProteinsSaccharomyces cerevisiae ProteinsTubulindepolymerizationkinesinsmicrotubule associated proteinsmicrotubule dynamicsspindle scaling

Identifiers

PMID28697331
PMCPMC5573156
OpenAlexW2735920617

What OpenQuestion holds

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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.