title: Novel calcineurin interacting protein-2: the functional characterization of CNP-2 in Caenorhabditis elegans.
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.
authors.affiliation: Department of Life Science, Gwangju Institute of Science and Technology, Gwangju, Korea.
authors.forename: Cai
authors.initials: C
authors.lastname: Xianglan
authors.forename: Kyung Min
authors.initials: KM
authors.lastname: Ko
authors.forename: Gunasekaran
authors.initials: G
authors.lastname: Singaravelu
authors.forename: Joohong
authors.initials: J
authors.lastname: Ahnn
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D017173:Caenorhabditis elegans / Q000378:metabolism*; D029742:Caenorhabditis elegans Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D019703:Calcineurin / Q000378:metabolism*; D008969:Molecular Sequence Data; D011485:Protein Binding; D034622:RNA Interference; D017386:Sequence Homology, Amino Acid
chemical_list: D029742:Caenorhabditis elegans Proteins; D019703:Calcineurin