Molecular Biology of the Cell click for CBE Life Science Education Page

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


     

Originally published as MBC in Press, 10.1091/mbc.E04-09-0851 on November 24, 2004

Vol. 16, Issue 2, 458-469, February 2005

This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow All Versions of this Article:
E04-09-0851v1
16/2/458    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 HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Hu, J.
Right arrow Articles by Barr, M. M.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Hu, J.
Right arrow Articles by Barr, M. M.

ATP-2 Interacts with the PLAT Domain of LOV-1 and Is Involved in Caenorhabditis elegans Polycystin Signaling

Jinghua Hu, and Maureen M. Barr *

Division of Pharmaceutical Sciences, School of Pharmacy, University of Wisconsin-Madison, Madison, WI 53705

Submitted September 29, 2004; Revised November 10, 2004; Accepted November 16, 2004
Monitoring Editor: Martin Chalfie

Caenorhabditis elegans is a powerful model to study the molecular basis of autosomal dominant polycystic kidney disease (ADPKD). ADPKD is caused by mutations in the polycystic kidney disease (PKD)1 or PKD2 gene, encoding polycystin (PC)-1 or PC-2, respectively. The C. elegans polycystins LOV-1 and PKD-2 are required for male mating behaviors and are localized to sensory cilia. The function of the evolutionarily conserved polycystin/lipoxygenase/{alpha}-toxin (PLAT) domain found in all PC-1 family members remains an enigma. Here, we report that ATP-2, the {beta} subunit of the ATP synthase, physically associates with the LOV-1 PLAT domain and that this interaction is evolutionarily conserved. In addition to the expected mitochondria localization, ATP-2 and other ATP synthase components colocalize with LOV-1 and PKD-2 in cilia. Disrupting the function of the ATP synthase or overexpression of atp-2 results in a male mating behavior defect. We further show that atp-2, lov-1, and pkd-2 act in the same molecular pathway. We propose that the ciliary localized ATP synthase may play a previously unsuspected role in polycystin signaling.

Article published online ahead of print in MBC in Press on November 24, 2004 (http://www.molbiolcell.org/cgi/doi/10.1091/mbc.E04-09-0851).

* Corresponding author. E-mail address: mmbarr{at}pharmacy.wisc.edu.




This article has been cited by other articles:


Home page
 Mol. Biol. CellHome page
J. Hu, S. G. Wittekind, and M. M. Barr
STAM and Hrs Down-Regulate Ciliary TRP Receptors
Mol. Biol. Cell, September 1, 2007; 18(9): 3277 - 3289.
[Abstract] [Full Text] [PDF]

Home page
 Mol. Biol. CellHome page
J. Hu, Y.-K. Bae, K. M. Knobel, and M. M. Barr
Casein Kinase II and Calcineurin Modulate TRPP Function and Ciliary Localization
Mol. Biol. Cell, May 1, 2006; 17(5): 2200 - 2211.
[Abstract] [Full Text] [PDF]

Home page
 Am. J. Physiol. Renal Physiol.Home page
J. R. Davenport and B. K. Yoder
An incredible decade for the primary cilium: a look at a once-forgotten organelle
Am J Physiol Renal Physiol, December 1, 2005; 289(6): F1159 - F1169.
[Abstract] [Full Text] [PDF]


Home Help [Feedback] [For Subscribers] [Archive] [Search] [Contents]
Copyright © 2005 by The American Society for Cell Biology. Terms of copyright protection, warranties, and disclaimers.