Regulation of flagellar dynein activity by a central pair kinesin.

Abstract:

:The motility of cilia and flagella is powered by dynein ATPases associated with outer doublet microtubules. However, a flagellar kinesin-like protein that may function as a motor associates with the central pair complex. We determined that Chlamydomonas reinhardtii central pair kinesin Klp1 is a phosphoprotein and, like conventional kinesins, binds to microtubules in vitro in the presence of adenosine 5'-[beta,gamma-imido]triphosphate, but not ATP. To characterize the function of Klp1, we generated RNA interference expression constructs that reduce in vivo flagellar Klp1 levels. Klp1 knockdown cells have flagella that either beat very slowly or are paralyzed. EM image averages show disruption of two structures associated with the C2 central pair microtubule, C2b and C2c. Greatest density is lost from part of projection C2c, which is in a position to interact with doublet-associated radial spokes. Klp1 therefore retains properties of a motor protein and is essential for normal flagellar motility. We hypothesize that Klp1 acts as a conformational switch to signal spoke-dependent control of dynein activity.

authors

Yokoyama R,O'toole E,Ghosh S,Mitchell DR

doi

10.1073/pnas.0406817101

keywords:

subject

Has Abstract

pub_date

2004-12-14 00:00:00

pages

17398-403

issue

50

eissn

0027-8424

issn

1091-6490

pii

0406817101

journal_volume

101

pub_type

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