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A Novel Calcineurin-interacting Protein, CNP-3, Modulates Calcineurin Deficient Phenotypes in Caenorhabditis elegans  

Kim, Yun Hee (Department of Life Science, Gwangju Institute of Science and Technology)
Song, Hyun-Ok (Department of Life Science, Gwangju Institute of Science and Technology)
Ko, Kyung Min (Department of Life Science, Gwangju Institute of Science and Technology)
Singaravelu, Gunasekaran (Department of Life Science, Hanyang University)
Jee, Changhoon (Department of Life Science, Gwangju Institute of Science and Technology)
Kang, Junsu (Institute of Molecular Biology and Genetics, Department of Biological Sciences, Seoul National University)
Ahnn, Joohong (Department of Life Science, Hanyang University)
Publication Information
Molecules and Cells / v.25, no.4, 2008 , pp. 566-571 More about this Journal
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.
Keywords
Calcineurin (Cn); Calcineurin Binding Protein; C. elegans; CNP-3; TAX-6;
Citations & Related Records
Times Cited By KSCI : 1  (Citation Analysis)
Times Cited By Web Of Science : 3  (Related Records In Web of Science)
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