Evidence map›Paper›PMID 26150501›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2015

Biased Brownian motion as a mechanism to facilitate nanometer-scale exploration of the microtubule plus end by a kinesin-8.

Yongdae Shin, Yaqing Du, Scott E Collier, Melanie D Ohi, Matthew J Lang, Ryoma Ohi

Abstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing 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

14 citing papers in PubMed.

  1. International journal of molecular sciences · 2026
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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

6 authors.

Yongdae ShinDepartment of Mechanical Engineering, Massachusetts Institute of Technology, Cambridge, MA 02139;
Yaqing DuDepartment of Cell and Developmental Biology, Vanderbilt University Medical Center, Nashville, TN 37232;
Scott E CollierDepartment of Cell and Developmental Biology, Vanderbilt University Medical Center, Nashville, TN 37232;
Melanie D OhiDepartment of Cell and Developmental Biology, Vanderbilt University Medical Center, Nashville, TN 37232;
Matthew J LangDepartment of Chemical and Biomolecular Engineering, Vanderbilt University, Nashville, TN 37235; Department of Molecular Physiology and Biophysics, Vanderbilt University, Nashville, TN 37235 ryoma.ohi@vanderbilt.edu matt.lang@vanderbilt.edu.
Ryoma OhiDepartment of Cell and Developmental Biology, Vanderbilt University Medical Center, Nashville, TN 37232; ryoma.ohi@vanderbilt.edu matt.lang@vanderbilt.edu.

Funding

MOLECULAR BIOPHYSICS TRAINING PROGRAM AT VANDERBILTT32GM008320 · NIGMS · VANDERBILT UNIVERSITY · PI CHAZIN, WALTER J. · 1989 to 2023
$7.9M
Integrated Biological Systems Training in OncologyT32CA119925 · NCI · VANDERBILT UNIVERSITY · PI Vivian Gama, William Patrick Tansey · 2008 to 2026
$7.6M
Regulation of microtubule dynamics during cell divisionR01GM086610 · NIGMS · VANDERBILT UNIVERSITY · PI OHI, RYOMA · 2010 to 2023
$4.5M
Acquisition of a super-resolution optical microscopeS10OD012324 · OD · VANDERBILT UNIVERSITY · PI TYSKA, MATTHEW J · 2012 to 2012
$1.1M
Computational and single molecule analysis of kinesin's atomistic machineryR01GM087677 · NIGMS · TEXAS ENGINEERING EXPERIMENT STATION · PI HWANG, WONMUK, LANG, MATTHEW J. · 2009 to 2012
$911k
NCI NIH HHS T32 CA119925NIGMS NIH HHS R01 GM086610NIGMS NIH HHS R01GM086610NIGMS NIH HHS R01 GM087677NIGMS NIH HHS R01GM087677NIGMS NIH HHS T32 GM008320NIH HHS 1S10OD012324NIH HHS S10 OD012324
6 · The paper itself

Abstract

Kinesin-8s are plus-end-directed motors that negatively regulate microtubule (MT) length. Well-characterized members of this subfamily (Kip3, Kif18A) exhibit two important properties: (i) They are "ultraprocessive," a feature enabled by a second MT-binding site that tethers the motors to a MT track, and (ii) they dissociate infrequently from the plus end. Together, these characteristics combined with their plus-end motility cause Kip3 and Kif18A to enrich preferentially at the plus ends of long MTs, promoting MT catastrophes or pausing. Kif18B, an understudied human kinesin-8, also limits MT growth during mitosis. In contrast to Kif18A and Kip3, localization of Kif18B to plus ends relies on binding to the plus-end tracking protein EB1, making the relationship between its potential plus-end-directed motility and plus-end accumulation unclear. Using single-molecule assays, we show that Kif18B is only modestly processive and that the motor switches frequently between directed and diffusive modes of motility. Diffusion is promoted by the tail domain, which also contains a second MT-binding site that decreases the off rate of the motor from the MT lattice. In cells, Kif18B concentrates at the extreme tip of a subset of MTs, superseding EB1. Our data demonstrate that kinesin-8 motors use diverse design principles to target MT plus ends, which likely target them to the plus ends of distinct MT subpopulations in the mitotic spindle.

Indexed as

Biophysical PhenomenaMotionCell TrackingDiffusionHeLa CellsHumansKinesinsKineticsMicrotubulesMutant ProteinsProtein BindingProtein MultimerizationProtein Structure, TertiaryVideo RecordingKIF18B protein, humanKinesinsMutant ProteinsEB1Kif18Bkinesin-8microtubulemitosis

Identifiers

PMID26150501
PMCPMC4517267

What OpenQuestion holds

Textmetadata
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.