Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Catalysis of the microtubule on-rate is the major parameter regulating the depolymerase activity of MCAK.

Nature structural & molecular biology - 1 Jan 2010

Cooper Jeremy R, Wagenbach Michael, Asbury Charles L, Wordeman Linda

Abstract excerpt

The kinesin-13, MCAK, is a critical regulator of microtubule dynamics in eukaryotic cells. We have functionally dissected the structural features responsible for MCAK's potent microtubule depolymerization activity. MCAK's positively charged neck enhances its delivery to microtubule ends not by te...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Catalysis
Share to Cricetulus
Share to Dimerization

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Image Processing, Computer-Assisted

Share to Kinesins

Share to Microscopy, Fluorescence

Share to Microtubules

Share to Tubulin

Source

Open in PubMed Open full text

Identifiers

PMID: 19966798
DOI: 10.1038/nsmb.1728
PMCID: PMC2909650

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 2 Sept 2026. Prepared record publication-19966798-2026-09-02.2. Manifest publication-graph-cohort-2026-09-02.2.

Source receipt: PubMed via Helena Literature Corpus, retrieved 2 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Catalysis of the microtubule on-rate is the major parameter regulating the depolymerase activity of MCAK.PMID 19966798Read ↗

Modeling study of kinesin-13 MCAK microtubule depolymerase.Semantic proximity Read ↗

K-loop insertion restores microtubule depolymerizing activity of a "neckless" MCAK mutant.Semantic proximity Read ↗

The family-specific α4-helix of the kinesin-13, MCAK, is critical to microtubule end recognition.Semantic proximity Read ↗

Insight into microtubule disassembly by kinesin-13s from the structure of Kif2C bound to tubulin.Semantic proximity Read ↗

Structural model of microtubule dynamics inhibition by Kinesin-4 from the crystal structure of KLP-12 –tubulin complexSemantic proximity Read ↗

Tau directs intracellular trafficking by regulating the forces exerted by kinesin and dynein teamsSemantic proximity Read ↗

The yeast kinesin-5 Cin8 interacts with the microtubule in a noncanonical manner.Semantic proximity Read ↗

A kinesin motor in a force-producing conformation.Semantic proximity Read ↗

Role of kinesin-1-based microtubule sliding in Drosophila nervous system development.Semantic proximity Read ↗

Tug-of-war as a cooperative mechanism for bidirectional cargo transport by molecular motors.Semantic proximity Read ↗

Discrete regions of the kinesin-8 Kip3 tail differentially mediate astral microtubule stability and spindle disassembly.Semantic proximity Read ↗

Functional characterization of MCAK/Kif2C cancer mutations using high-throughput microscopic analysis.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.