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KMID : 0578320080250040566
Molecules and Cells
2008 Volume.25 No. 4 p.566 ~ p.571
A Novel Calcineurin-interacting Protein, CNP-3, Modulates Calcineurin Deficient Phenotypes in Caenorhabditis elegans
Kim Yun-Hee

Singaravelu Gunasekaran
Song Hyun-Ok
Ko Kyung-Min
Jee Chang-Hoon
Kang Jun-Su
Ahnn Joo-Hong
Abstract
Calcineurin (Cn) is a calcium/calmodulin-dependent serine/threonine protein phosphatase that has diverse functions in different cell types and organisms. We screened proteins interacting with the C. elegans CnA homolog, TAX-6, by the yeast two-hybrid system. CNP-3 (Calcineurin interacting protein-3) is a novel protein that physically interacts with the catalytic domain of TAX-6. It is strongly expressed in the nuclei of intestine, hypodermis, dorsal uterine regions and spermatheca. Expression begins around the 60-cell stage and proceeds during all larval stages and the adult. To elucidate the biological function of cnp-3 we isolated a cnp-3 deletion mutant. Since CNP-3 binds CnA, we looked at factors associated with calcineurin loss-of-function mutants, such as brood size, body size, serotonin- and levamisole-mediated egg-laying behavior. The cnp-3(jh145) single mutant had no gross defects compared to wild-type animal. However, the phenotypes of the double mutants, tax-6(p675);cnp-3(jh145) and cnb-1(jh103);cnp-3(jh145), were more severe in terms of brood size, body size and serotonin-mediated egg-laying defects than tax-6(p675) and cnb-1(jh103), respectively. These results suggest that dysfunction of cnp-3 enhances certain calcineurin loss-of-function phenotypes in C. elegans.
KEYWORD
Calcineurin (Cn), Calcineurin Binding Protein, elegans, C. CNP-3, TAX-6
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