Evidence map›Paper›PMID 17093055›Full record

ArticleMolecular biology of the cell2007

The interplay of the N- and C-terminal domains of MCAK control microtubule depolymerization activity and spindle assembly.

Stephanie C Ems-McClung, Kathleen M Hertzer, Xin Zhang, Mill W Miller, Claire E Walczak

Abstract read
In one paragraph

Article in Molecular biology of the cell, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.

0numbers the graph read from it
0cells of the map it votes in
31citing 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

31 citing papers in PubMed.

  1. KIF2C is essential for meiosis and manchette dynamics in male mice.Frontiers in cell and developmental biology · 2025
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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

5 authors.

Stephanie C Ems-McClungMedical Science Program, Indiana University, Bloomington, IN 47405, USA.
Kathleen M Hertzer
Xin Zhang
Mill W Miller
Claire E Walczak

Funding

TRAINING IN GENETICST32GM007757 · NIGMS · TRUSTEES OF INDIANA UNIVERSITY · PI KUMAR, JUSTIN P · 1985 to 2014
$8.1M
Mechanisms of Spindle AssemblyR01GM059618 · NIGMS · INDIANA UNIV-PURDUE UNIV AT INDIANAPOLIS · PI WALCZAK, CLAIRE E · 1999 to 2016
$4.7M
Analysis of Interactions Between Rev and MicrotubulesR15GM073688 · NIGMS · WRIGHT STATE UNIVERSITY · PI MILLER, MILL W · 2005 to 2005
$194k
NIGMS NIH HHS GM-007757NIGMS NIH HHS R01 GM059618NIGMS NIH HHS R01GM059618NIGMS NIH HHS R15 GM073688NIGMS NIH HHS R15GM073688-01NIGMS NIH HHS T32 GM007757
6 · The paper itself

Abstract

Spindle assembly and accurate chromosome segregation require the proper regulation of microtubule dynamics. MCAK, a Kinesin-13, catalytically depolymerizes microtubules, regulates physiological microtubule dynamics, and is the major catastrophe factor in egg extracts. Purified GFP-tagged MCAK domain mutants were assayed to address how the different MCAK domains contribute to in vitro microtubule depolymerization activity and physiological spindle assembly activity in egg extracts. Our biochemical results demonstrate that both the neck and the C-terminal domain are necessary for robust in vitro microtubule depolymerization activity. In particular, the neck is essential for microtubule end binding, and the C-terminal domain is essential for tight microtubule binding in the presence of excess tubulin heterodimer. Our physiological results illustrate that the N-terminal domain is essential for regulating microtubule dynamics, stimulating spindle bipolarity, and kinetochore targeting; whereas the C-terminal domain is necessary for robust microtubule depolymerization activity, limiting spindle bipolarity, and enhancing kinetochore targeting. Unexpectedly, robust MCAK microtubule (MT) depolymerization activity is not needed for sperm-induced spindle assembly. However, high activity is necessary for proper physiological MT dynamics as assayed by Ran-induced aster assembly. We propose that MCAK activity is spatially controlled by an interplay between the N- and C-terminal domains during spindle assembly.

Indexed as

AnimalsCell ExtractsKinesinsMaleMicrotubulesMutant ProteinsOvumProtein Structure, TertiaryProto-Oncogene Proteins c-mosSpermatozoaSpindle ApparatusXenopus laevisCell ExtractsKinesinsMutant ProteinsProto-Oncogene Proteins c-mos

Identifiers

PMID17093055
PMCPMC1751331

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.