Casein kinase 2 reverses tail-independent inactivation of kinesin-1

Jing Xu, Babu J. N. Reddy, Preetha Anand, Zhanyong Shu, Silvia Cermelli, Michelle K. Mattson, Suvranta K. Tripathy, Matthew T. Hoss, Nikita S. James, Stephen J. King, Lan Huang, Lee Bardwell and Steven P. Gross ()
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Jing Xu: University of California, Irvine
Babu J. N. Reddy: University of California, Irvine
Preetha Anand: University of California, Irvine
Zhanyong Shu: University of California, Irvine
Silvia Cermelli: University of California, Irvine
Michelle K. Mattson: University of California, Irvine
Suvranta K. Tripathy: University of California, Irvine
Matthew T. Hoss: University of California, Irvine
Nikita S. James: University of California, Irvine
Stephen J. King: Burnett School of Biomedical Sciences, University of Central Florida
Lan Huang: University of California, Irvine
Lee Bardwell: University of California, Irvine
Steven P. Gross: University of California, Irvine

Nature Communications, 2012, vol. 3, issue 1, 1-12

Abstract: Abstract Kinesin-1 is a plus-end microtubule-based motor, and defects in kinesin-based transport are linked to diseases including neurodegeneration. Kinesin can auto-inhibit via a head–tail interaction, but is believed to be active otherwise. Here we report a tail-independent inactivation of kinesin, reversible by the disease-relevant signalling protein, casein kinase 2 (CK2). The majority of initially active kinesin (native or tail-less) loses its ability to interact with microtubules in vitro, and CK2 reverses this inactivation (approximately fourfold) without altering kinesin's single motor properties. This activation pathway does not require motor phosphorylation, and is independent of head–tail auto-inhibition. In cultured mammalian cells, reducing CK2 expression, but not its kinase activity, decreases the force required to stall lipid droplet transport, consistent with a decreased number of active kinesin motors. Our results provide the first direct evidence of a protein kinase upregulating kinesin-based transport, and suggest a novel pathway for regulating the activity of cargo-bound kinesin.

Date: 2012
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DOI: 10.1038/ncomms1760

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