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Dynactin Enhances the Processivity of Kinesin‐2
Author(s) -
Berezuk Matthew A.,
Schroer Trina A.
Publication year - 2007
Publication title -
traffic
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.677
H-Index - 130
eISSN - 1600-0854
pISSN - 1398-9219
DOI - 10.1111/j.1600-0854.2006.00517.x
Subject(s) - processivity , kinesin , dynactin , microtubule , microbiology and biotechnology , biology , dynein , motor protein , biophysics , biochemistry , enzyme , polymerase
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.