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KMID : 0624620080410060455
BMB Reports
2008 Volume.41 No. 6 p.455 ~ p.460
Novel calcineurin interacting protein-2: the functional characterization of CNP-2 in Caenorhabditis elegans
Xianglan Cai

Ko Kyung-Min
Singaravelu Gunasekaran
Ahnn Joo-Hong
Abstract
Calcineurin (Cn) is a serine/threonine phosphatase implicated in a wide variety of biological responses. To identify proteins that mediate Cn signaling pathway effects, we used yeast two-hybrid assays to screen for Cn interacting proteins, discovering a protein encoded by the gene, cnp-2 (Y46G5A.10). Utilizing serially deleted forms of Cn as baits, we demonstrated that the catalytic domain of Cn (TAX-6) binds with CNP-2, and this physical interaction was able to be reconstituted in vitro, supporting our yeast two-hybrid results. cnp-2 is a nematode-specific novel gene found in C. elegans as well as its closest relative, C. briggsae. CNP-2 was strongly expressed in the intestine of C. elegans. To study the function of cnp-2, we performed cnp-2 RNAi knock-down and characterized phenotypes associated with Cn mutants. However, no gross defects were revealed in these RNAi experiments. CNP-2 was proven to be a Cn binding protein; however, its role remains to be elucidated. [BMB reports 2008; 41(6): 455-460]
KEYWORD
Calcineurin (Cn), Calcineurin binding protein, C. elegans, CNP-2, TAX-6
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