A novel calcineurin-interacting protein, CNP-3, modulates calcineurin deficient phenotypes in Caenorhabditis elegans

Yun Hee Kim, Hyun Ok Song, Kyung Min Ko, Gunasekaran Singaravelu, Changhoon Jee, Junsu Kang, Joohong Ahnn

Research output: Contribution to journalArticle

4 Citations (Scopus)

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.

Original languageEnglish
Pages (from-to)566-571
Number of pages6
JournalMolecules and cells
Volume25
Issue number4
StatePublished - 2008 Jun 30

Fingerprint

Calcineurin
Caenorhabditis elegans
Phenotype
Body Size
Proteins
Ovum
Serotonin
Levamisole
Two-Hybrid System Techniques
Wild Animals
Phosphoprotein Phosphatases
Subcutaneous Tissue
Calmodulin
Intestines
Catalytic Domain
Calcium

Keywords

  • C. elegans
  • Calcineurin (Cn)
  • Calcineurin binding protein
  • CNP-3
  • TAX-6

Cite this

Kim, Y. H., Song, H. O., Ko, K. M., Singaravelu, G., Jee, C., Kang, J., & Ahnn, J. (2008). A novel calcineurin-interacting protein, CNP-3, modulates calcineurin deficient phenotypes in Caenorhabditis elegans. Molecules and cells, 25(4), 566-571.
Kim, Yun Hee ; Song, Hyun Ok ; Ko, Kyung Min ; Singaravelu, Gunasekaran ; Jee, Changhoon ; Kang, Junsu ; Ahnn, Joohong. / A novel calcineurin-interacting protein, CNP-3, modulates calcineurin deficient phenotypes in Caenorhabditis elegans. In: Molecules and cells. 2008 ; Vol. 25, No. 4. pp. 566-571.
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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.",
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Kim, YH, Song, HO, Ko, KM, Singaravelu, G, Jee, C, Kang, J & Ahnn, J 2008, 'A novel calcineurin-interacting protein, CNP-3, modulates calcineurin deficient phenotypes in Caenorhabditis elegans', Molecules and cells, vol. 25, no. 4, pp. 566-571.

A novel calcineurin-interacting protein, CNP-3, modulates calcineurin deficient phenotypes in Caenorhabditis elegans. / Kim, Yun Hee; Song, Hyun Ok; Ko, Kyung Min; Singaravelu, Gunasekaran; Jee, Changhoon; Kang, Junsu; Ahnn, Joohong.

In: Molecules and cells, Vol. 25, No. 4, 30.06.2008, p. 566-571.

Research output: Contribution to journalArticle

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T1 - A novel calcineurin-interacting protein, CNP-3, modulates calcineurin deficient phenotypes in Caenorhabditis elegans

AU - Kim, Yun Hee

AU - Song, Hyun Ok

AU - Ko, Kyung Min

AU - Singaravelu, Gunasekaran

AU - Jee, Changhoon

AU - Kang, Junsu

AU - Ahnn, Joohong

PY - 2008/6/30

Y1 - 2008/6/30

N2 - 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.

AB - 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.

KW - C. elegans

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KW - Calcineurin binding protein

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Kim YH, Song HO, Ko KM, Singaravelu G, Jee C, Kang J et al. A novel calcineurin-interacting protein, CNP-3, modulates calcineurin deficient phenotypes in Caenorhabditis elegans. Molecules and cells. 2008 Jun 30;25(4):566-571.