Molecular Biology of the Cell Call for Nominations: MBC Editor-in-Chief

Home Help [Feedback] [For Subscribers] [Archive] [Search] --
QUICK SEARCH:   [advanced]


     

MBC in Press, published online ahead of print October 6, 2004
Mol. Biol. Cell 10.1091/mbc.E04-08-0694

A more recent version of this article appeared on December 1, 2004
This Article
Right arrow Full Text (PDF)
Right arrow All Versions of this Article:
E04-08-0694v1
15/12/5431    most recent
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Hendrickson, T. W.
Right arrow Articles by Sale, W. S.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Hendrickson, T. W.
Right arrow Articles by Sale, W. S.

Submitted on August 12, 2004
Revised on September 20, 2004
Accepted on September 22, 2004

IC138 is a WD-repeat Dynein Intermediate Chain Required for Light Chain Assembly and Regulation of Flagellar Bending

Triscia W. Hendrickson,* Catherine A. Perrone,{dagger} Paul Griffin,* Kristin Wuichet,* Joshua Mueller,{dagger} Pinfen Yang,{ddagger} Mary E. Porter,{dagger} and Winfield S. Sale*{sect}

*Department of Cell Biology, Emory University School of Medicine, Atlanta, GA 30322; {dagger}Department of Genetics/Cell and Developmental Biology, University of Minnesota, Minneapolis, MN 55455; {ddagger}Department of Biology, Marquette University, Milwaukee, WI 53201

Monitoring Editor: Thomas Pollard

Increased phosphorylation of dynein IC IC138 correlates with decreases in flagellar microtubule sliding and phototaxis defects. To test the hypothesis that regulation of IC138 phosphorylation controls flagellar bending, we cloned the IC138 gene. IC138 encodes a novel protein with a calculated mass of 111 kDa and is predicted to form seven WD-repeats at the C-terminus. IC138 maps near the BOP5 locus and bop5-1 contains a point mutation resulting in a truncated IC138 lacking the C-terminus, including the seventh WD-repeat. bop5-1 cells display wild-type flagellar beat frequency but swim slower than wild-type cells, suggesting that bop5-1 is altered in its ability to control flagellar waveform. Swimming speed is rescued in bop5-1 transformants containing the wild-type IC138, confirming that BOP5 encodes IC138. With the exception of the roadblock-related light chain, LC7b, all the other known components of the I1 complex, including the truncated IC138, are assembled in bop5-1 axonemes. Thus, the bop5-1 motility phenotype reveals a role for IC138 and LC7b in the control of flagellar bending. IC138 is hyperphosphorylated in paralyzed flagellar mutants lacking radial spoke and central pair components, further indicating a role for the radial spokes and central pair apparatus in control of IC138 phosphorylation and regulation of flagellar waveform.

{sect}Corresponding author. E-mail: win{at}cellbio.emory.edu






Home Help [Feedback] [For Subscribers] [Archive] [Search] --
Copyright © 2004 by The American Society for Cell Biology. Terms of copyright protection, warranties, and disclaimers.