CK2 activates kinesin via induction of a conformational change

Michelle K. Mattson-Hoss, Yamato Niitani, Elizabeth A. Gordon, Yonggun Jun, Lee Bardwell, Michio Tomishige, Steven P. Gross

Research output: Contribution to journalArticlepeer-review

6 Scopus citations


Kinesin is the canonical plus-end microtubule motor and has been the focus of intense study since its discovery in 1985. We previously demonstrated a time-dependent inactivation of kinesin in vitro that was fully reversible by the addition of purified casein kinase 2 (CK2) and showed that this inactivation/reactivation pathway was relevant in cells. Here we show that kinesin inactivation results from a conformational change that causes the neck linker to be positioned closer to the motor domain. Furthermore, we show that treatment of kinesin with CK2 prevents and reverses this repositioning. Finally, we demonstrate that CK2 treatment facilitates ADP dissociation from the motor, resulting in a nucleotidefree state that promotes microtubule binding. Thus, we propose that kinesin inactivation results from neck-linker repositioning and that CK2-mediated reactivation results from CK2's dual ability to reverse this repositioning and to promote ADP release.

Original languageEnglish
Pages (from-to)7000-7005
Number of pages6
JournalProceedings of the National Academy of Sciences of the United States of America
Issue number19
StatePublished - 13 May 2014


  • Cargo travel
  • Multiple-motor transport
  • Transport regulation


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