Regulation of flagellar dynein activity by a central pair kinesin

Proc Natl Acad Sci U S A. 2004 Dec 14;101(50):17398-403. doi: 10.1073/pnas.0406817101. Epub 2004 Nov 30.

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.

Publication types

  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Animals
  • Chlamydomonas reinhardtii / cytology
  • Chlamydomonas reinhardtii / genetics
  • Chlamydomonas reinhardtii / metabolism
  • Dyneins / metabolism*
  • Flagella / genetics
  • Flagella / metabolism*
  • Kinesin / genetics
  • Kinesin / metabolism*
  • Kinesin / ultrastructure
  • Microscopy, Electron
  • Microtubules / metabolism
  • Phosphorylation
  • RNA Interference

Substances

  • Dyneins
  • Kinesin