PMID: 8943017Nov 26, 1996Paper

Calexcitin: a signaling protein that binds calcium and GTP, inhibits potassium channels, and enhances membrane excitability

Proceedings of the National Academy of Sciences of the United States of America
T J NelsonD L Alkon

Abstract

A previously uncharacterized 22-kDa Ca(2+)-binding protein that also binds guanosine nucleotides was characterized, cloned, and analyzed by electrophysiological techniques. The cloned protein, calexcitin, contains two EF-hands and also has homology with GTP-binding proteins in the ADP ribosylation factor family. In addition to binding two molecules of Ca2+, calexcitin bound GTP and possessed GTPase activity. Calexictin is also a high affinity substrate for protein kinase C. Application of calexcitin to the inner surface of inside-out patches of human fibroblast membranes, in the presence of Ca2+ and the absence of endogenous Ca2+/calmodulin kinase type II or protein kinase C activity, reduced the mean open time and mean open probability of 115 +/- 6 pS K+ channels. Calexcitin thus appears to directly regulate K+ channels. When microinjected into molluscan neurons or rabbit cerebellar Purkinje cell dendrites, calexcitin was highly effective in enhancing membrane excitability. Because calexcitin translocates to the cell membrane after phosphorylation, calexcitin could serve as a Ca(2+)-activated signaling molecule that increases cellular excitability, which would in turn increase Ca2+ influx through the membrane. This is also the...Continue Reading

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Citations

Jul 24, 2002·Neuroscience Research·Ryo KawaiManabu Sakakibara
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Aug 2, 2003·Comparative Biochemistry and Physiology. Part B, Biochemistry & Molecular Biology·Thomas J NelsonDaniel L Alkon
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Dec 7, 2021·Acta Crystallographica. Section F, Structural Biology Communications·Jingxu GuoJonathan B Cooper

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