Structure of the Kinesin13-Microtubule Ring Complex

Dongyan Tan, William J. Rice, Hernando J. Sosa

Research output: Contribution to journalArticle

37 Citations (Scopus)

Abstract

To investigate the mechanism of kinesin13-induced microtubule depolymerization, we have calculated a three-dimensional (3D) map of the kinesin13-microtubule ring complex, using cryo-electron microscopy (cryo-EM) and image analysis. An atomic model of the complex was produced by docking the crystal structures of tubulin and a kinesin13 motor domain (MD) into the 3D map. The model reveals a snapshot of the depolymerization mechanism by providing a 3D view of the complex formed between the kinesin13 MD and a curved tubulin protofilament (pf). It suggests that contacts mediated by kinesin13 class-specific residues in the putative microtubule-binding site stabilize intra-dimer tubulin curvature. In addition, a tubulin-binding site on the kinesin13 MD was identified. Mutations at this class-conserved site selectively disrupt the formation of microtubule-associated ring complexes.

Original languageEnglish (US)
Pages (from-to)1732-1739
Number of pages8
JournalStructure
Volume16
Issue number11
DOIs
StatePublished - Nov 12 2008

Fingerprint

Tubulin
Microtubules
Binding Sites
Cryoelectron Microscopy
Mutation

Keywords

  • CELLBIO
  • PROTEINS

ASJC Scopus subject areas

  • Molecular Biology
  • Structural Biology

Cite this

Structure of the Kinesin13-Microtubule Ring Complex. / Tan, Dongyan; Rice, William J.; Sosa, Hernando J.

In: Structure, Vol. 16, No. 11, 12.11.2008, p. 1732-1739.

Research output: Contribution to journalArticle

Tan, Dongyan ; Rice, William J. ; Sosa, Hernando J. / Structure of the Kinesin13-Microtubule Ring Complex. In: Structure. 2008 ; Vol. 16, No. 11. pp. 1732-1739.
@article{121188eb9bb54bf59283a13a30d3d02a,
title = "Structure of the Kinesin13-Microtubule Ring Complex",
abstract = "To investigate the mechanism of kinesin13-induced microtubule depolymerization, we have calculated a three-dimensional (3D) map of the kinesin13-microtubule ring complex, using cryo-electron microscopy (cryo-EM) and image analysis. An atomic model of the complex was produced by docking the crystal structures of tubulin and a kinesin13 motor domain (MD) into the 3D map. The model reveals a snapshot of the depolymerization mechanism by providing a 3D view of the complex formed between the kinesin13 MD and a curved tubulin protofilament (pf). It suggests that contacts mediated by kinesin13 class-specific residues in the putative microtubule-binding site stabilize intra-dimer tubulin curvature. In addition, a tubulin-binding site on the kinesin13 MD was identified. Mutations at this class-conserved site selectively disrupt the formation of microtubule-associated ring complexes.",
keywords = "CELLBIO, PROTEINS",
author = "Dongyan Tan and Rice, {William J.} and Sosa, {Hernando J.}",
year = "2008",
month = "11",
day = "12",
doi = "10.1016/j.str.2008.08.017",
language = "English (US)",
volume = "16",
pages = "1732--1739",
journal = "Structure with Folding & design",
issn = "0969-2126",
publisher = "Cell Press",
number = "11",

}

TY - JOUR

T1 - Structure of the Kinesin13-Microtubule Ring Complex

AU - Tan, Dongyan

AU - Rice, William J.

AU - Sosa, Hernando J.

PY - 2008/11/12

Y1 - 2008/11/12

N2 - To investigate the mechanism of kinesin13-induced microtubule depolymerization, we have calculated a three-dimensional (3D) map of the kinesin13-microtubule ring complex, using cryo-electron microscopy (cryo-EM) and image analysis. An atomic model of the complex was produced by docking the crystal structures of tubulin and a kinesin13 motor domain (MD) into the 3D map. The model reveals a snapshot of the depolymerization mechanism by providing a 3D view of the complex formed between the kinesin13 MD and a curved tubulin protofilament (pf). It suggests that contacts mediated by kinesin13 class-specific residues in the putative microtubule-binding site stabilize intra-dimer tubulin curvature. In addition, a tubulin-binding site on the kinesin13 MD was identified. Mutations at this class-conserved site selectively disrupt the formation of microtubule-associated ring complexes.

AB - To investigate the mechanism of kinesin13-induced microtubule depolymerization, we have calculated a three-dimensional (3D) map of the kinesin13-microtubule ring complex, using cryo-electron microscopy (cryo-EM) and image analysis. An atomic model of the complex was produced by docking the crystal structures of tubulin and a kinesin13 motor domain (MD) into the 3D map. The model reveals a snapshot of the depolymerization mechanism by providing a 3D view of the complex formed between the kinesin13 MD and a curved tubulin protofilament (pf). It suggests that contacts mediated by kinesin13 class-specific residues in the putative microtubule-binding site stabilize intra-dimer tubulin curvature. In addition, a tubulin-binding site on the kinesin13 MD was identified. Mutations at this class-conserved site selectively disrupt the formation of microtubule-associated ring complexes.

KW - CELLBIO

KW - PROTEINS

UR - http://www.scopus.com/inward/record.url?scp=55249105259&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=55249105259&partnerID=8YFLogxK

U2 - 10.1016/j.str.2008.08.017

DO - 10.1016/j.str.2008.08.017

M3 - Article

VL - 16

SP - 1732

EP - 1739

JO - Structure with Folding & design

JF - Structure with Folding & design

SN - 0969-2126

IS - 11

ER -