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Vol. 13, Issue 9, 3281-3293, September 2002

Calcineurin, a Calcium/Calmodulin-dependent Protein Phosphatase, Is Involved in Movement, Fertility, Egg Laying, and Growth in Caenorhabditis elegans

Jaya Bandyopadhyay,*dagger Dagger Jiyeon Lee,*Dagger Jungsoo Lee,*Dagger Jin Il Lee,* Jae-Ran Yu,§ Changhoon Jee,* Jeong-Hoon Cho,* Sunki Jung,* Myon Hee Lee, Sonia Zannoni,# Andrew Singson,# Do Han Kim,* Hyeon-Sook Koo, and Joohong Ahnn*||

 *Department of Life Science, Kwangju Institute of Science and Technology, Kwangju 500-712, Korea;  §Department of Parasitology, College of Medicine, Kon-Kuk University, Chungju 380-710, Korea;  Department of Biochemistry, College of Science, Yonsei University, Seoul 120-749, Korea; and  #Waksman Institute, Rutgers University, Piscataway, New Jersey 08854

Calcineurin is a Ca2+-calmodulin-dependent serine/threonine protein phosphatase that has been implicated in various signaling pathways. Here we report the identification and characterization of calcineurin genes in Caenorhabditis elegans (cna-1 and cnb-1), which share high homology with Drosophila and mammalian calcineurin genes. C. elegans calcineurin binds calcium and functions as a heterodimeric protein phosphatase establishing its biochemical conservation in the nematode. Calcineurin is expressed in hypodermal seam cells, body-wall muscle, vulva muscle, neuronal cells, and in sperm and the spermatheca. cnb-1 mutants showed pleiotropic defects including lethargic movement and delayed egg-laying. Interestingly, these characteristic defects resembled phenotypes observed in gain-of-function mutants of unc-43/Ca2+-calmodulin-dependent protein kinase II (CaMKII) and goa-1/Go-protein alpha -subunit. Double mutants of cnb-1 and unc-43(gf) displayed an apparent synergistic severity of movement and egg-laying defects, suggesting that calcineurin may have an antagonistic role in CaMKII-regulated phosphorylation signaling pathways in C. elegans.


|| Corresponding author. E-mail address: joohong{at}kjist.ac.kr.

Dagger These authors contributed equally to this work.

dagger Present address: Indian Institute of Chemical Biology, Calcutta, 700-032, India.


Molecular Biology of the Cell
Vol. 13, 3281-3293, September 2002
Copyright © 2002 by The American Society for Cell Biology



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