Evidence map›Paper›PMID 25485082›Full record

ArticleInterface focus2014

Molecular mechanisms for microtubule length regulation by kinesin-8 and XMAP215 proteins.

Louis Reese, Anna Melbinger, Erwin Frey

Open access · bronzeAbstract read
In one paragraph

Article in Interface focus, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.

0numbers the graph read from it
0cells of the map it votes in
7citing papers in PubMed
1.2field-weighted citation impact, top 24% 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

7 citing papers in PubMed, 24 citations in OpenAlex.

  1. Article
  2. Motor guidance by long-range communication on the microtubule highway.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  3. Article
  4. Altered nuclear dynamics in MDX myofibers.Journal of applied physiology (Bethesda, Md. : 1985) · 2017
    Article
  5. Article
  6. Review
  7. 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

3 authors at 1 institution in 2 countries.

Louis ReeseArnold Sommerfeld Center for Theoretical Physics and Center for NanoScience, Department of Physics , Ludwig-Maximilians-Universität München , Theresienstraße 37, 80333 Munich , Germany ; Nanosystems Initiative Munich (NIM) , Ludwig-Maximilians-Universität München , Schellingstraße 4, 80333 Munich , Germany.ORCID 0000-0002-0818-900X
Anna MelbingerArnold Sommerfeld Center for Theoretical Physics and Center for NanoScience, Department of Physics , Ludwig-Maximilians-Universität München , Theresienstraße 37, 80333 Munich , Germany ; Department of Physics , University of California , San Diego, CA 92093 , USA.
Erwin FreyArnold Sommerfeld Center for Theoretical Physics and Center for NanoScience, Department of Physics , Ludwig-Maximilians-Universität München , Theresienstraße 37, 80333 Munich , Germany ; Nanosystems Initiative Munich (NIM) , Ludwig-Maximilians-Universität München , Schellingstraße 4, 80333 Munich , Germany.
BMW (Germany) · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The cytoskeleton is regulated by a plethora of enzymes that influence the stability and dynamics of cytoskeletal filaments. How microtubules (MTs) are controlled is of particular importance for mitosis, during which dynamic MTs are responsible for proper segregation of chromosomes. Molecular motors of the kinesin-8 protein family have been shown to depolymerize MTs in a length-dependent manner, and recent experimental and theoretical evidence suggests a possible role for kinesin-8 in the dynamic regulation of MTs. However, so far the detailed molecular mechanisms of how these molecular motors interact with the growing MT tip remain elusive. Here we show that two distinct scenarios for the interactions of kinesin-8 with the MT tip lead to qualitatively different MT dynamics, including accurate length control as well as intermittent dynamics. We give a comprehensive analysis of the regimes where length regulation is possible and characterize how the stationary length depends on the biochemical rates and the bulk concentrations of the various proteins. For a neutral scenario, where MTs grow irrespective of whether the MT tip is occupied by a molecular motor, length regulation is possible only for a narrow range of biochemical rates, and, in particular, limited to small polymerization rates. By contrast, for an inhibition scenario, where the presence of a motor at the MT tip inhibits MT growth, the regime where length regulation is possible is extremely broad and includes high growth rates. These results also apply to situations where a polymerizing enzyme like XMAP215 and kinesin-8 mutually exclude each other from the MT tip. Moreover, we characterize the differences in the stochastic length dynamics between the two scenarios. While for the neutral scenario length is tightly controlled, length dynamics is intermittent for the inhibition scenario and exhibits extended periods of MT growth and shrinkage. On a broader perspective, the set of models established in this work quite generally suggest that mutual exclusion of molecules at the ends of cytoskeletal filaments is an important factor for filament dynamics and regulation.

Indexed as

kinesin-8microtubule dynamicsmolecular motorsXMAP215

Identifiers

PMID25485082
PMCPMC4213447
OpenAlexW1978209911

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.