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The mitotic kinesin-14 KlpA contains a context-dependent directionality switch
Andrew R Popchock1, Kuo-Fu Tseng2, Pan Wang2,3
1Department of Biochemistry and Biophysics, Oregon State University, Corvallis, Oregon 97331, USA.
Nature Communications
|January 5, 2017
Summary
Kinesin-14 motor KlpA from Aspergillus nidulans acts as a bidirectional motor. Its N-terminal tail controls directionality, enabling plus-end-directed movement on single microtubules.
Area of Science:
- Cell Biology
- Molecular Motors
- Cytoskeleton Dynamics
Background:
- Kinesin-14s are typically minus end-directed microtubule motors.
- They play crucial roles in mitotic spindle assembly.
Purpose of the Study:
- To investigate the motility of KlpA, a kinesin-14 from Aspergillus nidulans.
- To determine the factors influencing KlpA's directionality and processivity.
Main Methods:
- Total internal reflection fluorescence microscopy.
- Microtubule gliding assays.
- Microtubule sliding assays.
Main Results:
- KlpA exhibits context-dependent bidirectional motility.
- On single microtubules, KlpA shows plus end-directed processive movement, dependent on its N-terminal tail.
- When anchored or interacting with paired microtubules, KlpA displays minus end-directed motility.
Conclusions:
- KlpA functions as a bidirectional motor.
- The N-terminal tail acts as a directionality switch, regulating KlpA's movement based on its binding context.
