Unknown

Dataset Information

0

Cloning and characterization of a potassium-dependent sodium/calcium exchanger in Drosophila.


ABSTRACT: Sodium/calcium(-potassium) exchangers (NCX and NCKX) are critical for the rapid extrusion of calcium, which follows the stimulation of a variety of excitable cells. To further understand the mechanisms of calcium regulation in signaling, we have cloned a Drosophila sodium/calcium-potassium exchanger, Nckx30C. The overall deduced protein topology for NCKX30C is similar to that of mammalian NCKX, having five membrane-spanning domains in the NH(2) terminus separated from six at the COOH-terminal end by a large intracellular loop. We show that NCKX30C functions as a potassium-dependent sodium/calcium exchanger, and is not only expressed in adult neurons as was expected, but is also expressed during ventral nerve cord development in the embryo and in larval imaginal discs. Nckx30C is expressed in a dorsal-ventral pattern in the eye-antennal disc in a pattern that is similar to, but broader than that of wingless, suggesting that large fluxes of calcium may be occurring during imaginal disc development. Nckx30C may not only function in the removal of calcium and maintenance of calcium homeostasis during signaling in the adult, but may also play a critical role in signaling during development.

SUBMITTER: Haug-Collet K 

PROVIDER: S-EPMC2151195 | biostudies-literature | 1999 Nov

REPOSITORIES: biostudies-literature

altmetric image

Publications

Cloning and characterization of a potassium-dependent sodium/calcium exchanger in Drosophila.

Haug-Collet K K   Pearson B B   Webel R R   Szerencsei R T RT   Winkfein R J RJ   Schnetkamp P P PP   Colley N J NJ  

The Journal of cell biology 19991101 3


Sodium/calcium(-potassium) exchangers (NCX and NCKX) are critical for the rapid extrusion of calcium, which follows the stimulation of a variety of excitable cells. To further understand the mechanisms of calcium regulation in signaling, we have cloned a Drosophila sodium/calcium-potassium exchanger, Nckx30C. The overall deduced protein topology for NCKX30C is similar to that of mammalian NCKX, having five membrane-spanning domains in the NH(2) terminus separated from six at the COOH-terminal en  ...[more]

Similar Datasets

| S-EPMC6772386 | biostudies-literature
| S-EPMC3535175 | biostudies-literature
| S-EPMC3567274 | biostudies-literature
| S-EPMC6671846 | biostudies-literature
| S-EPMC3323054 | biostudies-literature
| S-EPMC7326190 | biostudies-literature
| S-EPMC3951392 | biostudies-literature
| S-EPMC9939835 | biostudies-literature
| S-EPMC2679901 | biostudies-literature
| S-EPMC2488271 | biostudies-literature