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CK2 activates kinesin via induction of a conformational change.

Abstract：

: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.

journal_name

Proc Natl Acad Sci U S A

journal_title

Proceedings of the National Academy of Sciences of the United States of America

authors

Mattson-Hoss MK,Niitani Y,Gordon EA,Jun Y,Bardwell L,Tomishige M,Gross SP

doi

10.1073/pnas.1321419111

subject

Has Abstract

pub_date

2014-05-13 00:00:00

pages

7000-5

issue

19

eissn

0027-8424

issn

1091-6490

pii

1321419111

journal_volume

111

pub_type

杂志文章

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