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- Title
Dynactin enhances the processivity of kinesin-2.
- Authors
Berezuk, Matthew A; Schroer, Trina A
- Abstract
Kinesin-2 is a major microtubule-based motor in most cell types. Its in vitro motile properties have been analyzed extensively and been found to differ considerably from kinesin-1. Although recombinant kinesin-2 heterodimers exhibit processive movement, the processivity of the native kinesin-2 holoenzyme has never been evaluated. Kinesin-2 can interact with dynactin, a 'processivity factor' for cytoplasmic dynein, which may alter its motile properties. In this study, we analyze the in vitro motility of single native kinesin-2 molecules and determine the effects of dynactin on motor processivity. We find that individual native kinesin-2 molecules travel processively. Dynactin has no effect on velocity but significantly increases the run length of kinesin-2 movements. These results show that the interaction with dynactin has important functional consequences on the activity of the kinesin-2 motor.
- Publication
Traffic (Copenhagen, Denmark), 2007, Vol 8, Issue 2, p124
- ISSN
1398-9219
- Publication type
Journal Article
- DOI
10.1111/j.1600-0854.2006.00517.x