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A mechanism for microtubule depolymerization by kini kinesins

Academic Article
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Overview

authors

  • Moores, C. A.
  • Yu, M.
  • Guo, J.
  • Beraud, C.
  • Sakowicz, R.
  • Milligan, Ronald

publication date

  • April 2002

journal

  • Molecular Cell  Journal

abstract

  • Whereas most kinesins motor along microtubules, KinI kinesins are microtubule depolymerizing machines. Surprisingly, we found that a KinI fragment consisting of only the motor core is capable of ATP-dependent depolymerization. The motor binds along microtubules in all nucleotide states, but in the presence of AMPPNP, microtubule depolymerization also occurs. Structural characterization of the products of AMPPNP-induced destabilization revealed a snapshot of the disassembly machine in action as it precisely deformed a tubulin dimer. While conventional kinesins use the energy of ATP binding to execute a "powerstroke," KinIs use it to bend the underlying protofilament. Thus, the relatively small class-specific differences within the KinI motor core modulate a fundamentally conserved mode of interaction with microtubules to produce a unique depolymerizing activity.

subject areas

  • Adenosine Triphosphate
  • Adenylyl Imidodiphosphate
  • Animals
  • Biomechanical Phenomena
  • Biopolymers
  • Dimerization
  • Kinesin
  • Macromolecular Substances
  • Microscopy, Electron
  • Microtubules
  • Models, Chemical
  • Models, Molecular
  • Molecular Motor Proteins
  • Peptide Fragments
  • Plasmodium falciparum
  • Protein Conformation
  • Protein Interaction Mapping
  • Protein Structure, Tertiary
  • Protozoan Proteins
  • Recombinant Fusion Proteins
  • Tubulin
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Identity

International Standard Serial Number (ISSN)

  • 1097-2765

Digital Object Identifier (DOI)

  • 10.1016/s1097-2765(02)00503-8

PubMed ID

  • 11983180
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Additional Document Info

start page

  • 903

end page

  • 909

volume

  • 9

issue

  • 4

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