Evidence map›Paper›PMID 29045878›Full record

ArticleBiophysical journal2017

Homodimeric Kinesin-2 KIF3CC Promotes Microtubule Dynamics.

Stephanie Guzik-Lendrum, Ivan Rayment, Susan P Gilbert

Open access · bronzeAbstract read
In one paragraph

Article in Biophysical journal, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed, 1 pooled it
1.4field-weighted citation impact, top 20% 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

11 citing papers in PubMed, 1 synthesis or guideline pooled it, 15 citations in OpenAlex.

  1. Pooled it
  2. Article
  3. Article
  4. Article
  5. The mechanochemistry of the kinesin-2 KIF3AC heterodimer is related to strain-dependent kinetic properties of KIF3A and KIF3C.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  6. Article
  7. Article
  8. Review
  9. Article
  10. Microtubule dynamics: an interplay of biochemistry and mechanics.Nature reviews. Molecular cell biology · 2018
    Review
  11. Kinesin-2 motors: Kinetics and biophysics.The Journal of biological chemistry · 2018
    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

3 authors at 2 institutions in 1 country.

Stephanie Guzik-LendrumDepartment of Biological Sciences and the Center for Biotechnology and Interdisciplinary Studies, Rensselaer Polytechnic Institute, Troy, New York.
Ivan RaymentDepartment of Biochemistry, University of Wisconsin, Madison, Wisconsin.
Susan P GilbertDepartment of Biological Sciences and the Center for Biotechnology and Interdisciplinary Studies, Rensselaer Polytechnic Institute, Troy, New York. Electronic address: sgilbert@rpi.edu.
Rensselaer Polytechnic Institute · USUniversity of Wisconsin–Madison · US

Funding

Mechanistic Analysis of Microtubule Based MotorsR37GM054141 · NIGMS · RENSSELAER POLYTECHNIC INSTITUTE · PI GILBERT, SUSAN P. · 2013 to 2022
$4.4M
NIGMS NIH HHS R37 GM054141
6 · The paper itself

Abstract

KIF3C is one subunit of the functional microtubule-based kinesin-2 KIF3AC motor, an anterograde cargo transporter in neurons. However, KIF3C has also been implicated as an injury-specific kinesin that is a key regulator of axonal growth and regeneration by promoting microtubule dynamics for reorganization at the neuronal growth cone. To test its potential role as a modulator of microtubule dynamics in vitro, an engineered homodimeric KIF3CC was incorporated into a dynamic microtubule assay and examined by total internal reflection fluorescence microscopy. The results reveal that KIF3CC is targeted to the microtubule plus-end, acts as a potent catastrophe factor through an increase in microtubule catastrophe frequency, and does so by elimination of the dependence of the catastrophe rate on microtubule lifetime. Moreover, KIF3CC accelerates the catastrophe rate without altering the microtubule growth rate. Therefore, the ATP-promoted KIF3CC mechanism of catastrophe is different from the well-described catastrophe factors kinesin-13 MCAK and kinesin-8 Kip3/KIF18A. The properties of KIF3CC were not shared by heterodimeric KIF3AC and required the unique KIF3C-specific sequence extension in loop L11 at the microtubule interface. At the microtubule plus-end, the presence of KIF3CC resulted in modulation of the tapered structure typically seen in growing dynamic microtubules to microtubule blunt plus-ends. Overall our results implicate homodimeric KIF3CC as a unique promoter of microtubule catastrophe and substantiate its physiological role in cytoskeletal remodeling.

Indexed as

Adenosine TriphosphateAnimalsKinesinsKineticsMiceMicroscopy, FluorescenceMicrotubulesModels, MolecularProtein MultimerizationAdenosine TriphosphateKif3a protein, mouseKif3c protein, mouseKinesins

Identifiers

PMID29045878
PMCPMC5647625
OpenAlexW2767195050

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.