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A mechanism for microtubule depolymerization by KinI kinesins.

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.

journal_name

Mol Cell

journal_title

Molecular cell

authors

Moores CA,Yu M,Guo J,Beraud C,Sakowicz R,Milligan RA

doi

10.1016/s1097-2765(02)00503-8

subject

Has Abstract

pub_date

2002-04-01 00:00:00

pages

903-9

issue

4

eissn

1097-2765

issn

1097-4164

pii

S1097-2765(02)00503-8

journal_volume

9

pub_type

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