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




*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
-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.
These authors contributed equally to this work.
Present address: Indian Institute of Chemical
Biology, Calcutta, 700-032, India.
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