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TitleInsight into the molecular mechanism of the multitasking kinesin-8 motor.
Journal, issue, pagesEMBO J, Vol. 29, Issue 20, Page 3437-3447, Year 2010
Publish dateOct 20, 2010
AuthorsCarsten Peters / Katjuša Brejc / Lisa Belmont / Andrew J Bodey / Yan Lee / Ming Yu / Jun Guo / Roman Sakowicz / James Hartman / Carolyn A Moores /
PubMed AbstractMembers of the kinesin-8 motor class have the remarkable ability to both walk towards microtubule plus-ends and depolymerise these ends on arrival, thereby regulating microtubule length. To analyse ...Members of the kinesin-8 motor class have the remarkable ability to both walk towards microtubule plus-ends and depolymerise these ends on arrival, thereby regulating microtubule length. To analyse how kinesin-8 multitasks, we studied the structure and function of the kinesin-8 motor domain. We determined the first crystal structure of a kinesin-8 and used cryo-electron microscopy to calculate the structure of the microtubule-bound motor. Microtubule-bound kinesin-8 reveals a new conformation compared with the crystal structure, including a bent conformation of the α4 relay helix and ordering of functionally important loops. The kinesin-8 motor domain does not depolymerise stabilised microtubules with ATP but does form tubulin rings in the presence of a non-hydrolysable ATP analogue. This shows that, by collaborating, kinesin-8 motor domain molecules can release tubulin from microtubules, and that they have a similar mechanical effect on microtubule ends as kinesin-13, which enables depolymerisation. Our data reveal aspects of the molecular mechanism of kinesin-8 motors that contribute to their unique dual motile and depolymerising functions, which are adapted to control microtubule length.
External linksEMBO J / PubMed:20818331 / PubMed Central
MethodsEM (helical sym.) / X-ray diffraction
Resolution2.2 - 13.0 Å
Structure data

EMDB-1701:
The molecular mechanism of the multi-tasking kinesin-8 motor
Method: EM (helical sym.) / Resolution: 10.1 Å

EMDB-1702:
Kif18A (ATP state) head bound to a microtubule
Method: EM (helical sym.) / Resolution: 13.0 Å

PDB-3lre:
Crystal Structure Analysis of Human Kinesin-8 Motor Domain
Method: X-RAY DIFFRACTION / Resolution: 2.2 Å

Chemicals

ChemComp-MG:
Unknown entry

ChemComp-ADP:
ADENOSINE-5'-DIPHOSPHATE / ADP, energy-carrying molecule*YM / Adenosine diphosphate

ChemComp-HOH:
WATER / Water

Source
  • homo sapiens (human)
  • Bos taurus (cattle)
KeywordsMOTOR PROTEIN / nucleotide binding / microtubule binding / ATP-binding / Cell projection / Cytoskeleton / Glycoprotein / Microtubule / Nucleotide-binding / Nucleus / Phosphoprotein / Protein transport / Transport

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