論文

査読有り
2014年5月

CK2 activates kinesin via induction of a conformational change

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
  • Michelle K. Mattson-Hoss
  • ,
  • Yamato Niitani
  • ,
  • Elizabeth A. Gordon
  • ,
  • Yonggun Jun
  • ,
  • Lee Bardwell
  • ,
  • Michio Tomishige
  • ,
  • Steven P. Gross

111
19
開始ページ
7000
終了ページ
7005
記述言語
英語
掲載種別
研究論文(学術雑誌)
DOI
10.1073/pnas.1321419111
出版者・発行元
NATL ACAD SCIENCES

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 nucleotide-free 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.

Web of Science ® 被引用回数 : 6

リンク情報
DOI
https://doi.org/10.1073/pnas.1321419111
PubMed
https://www.ncbi.nlm.nih.gov/pubmed/24782540
Web of Science
https://gateway.webofknowledge.com/gateway/Gateway.cgi?GWVersion=2&SrcAuth=JSTA_CEL&SrcApp=J_Gate_JST&DestLinkType=FullRecord&KeyUT=WOS:000335798000062&DestApp=WOS_CPL

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