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Calcium-dependent binding of calmodulin to neuronal gap junction proteins.

Abstract：

:We examined the interactions of calmodulin with neuronal gap junction proteins connexin35 (Cx35) from perch, its mouse homologue Cx36, and the related perch Cx34.7 using surface plasmon resonance. Calmodulin bound to the C-terminal domains of all three connexins with rapid kinetics in a concentration- and Ca2+-dependent manner. Dissociation was also very rapid. K(d)'s for calmodulin binding at a high-affinity site ranged from 11 to 72 nM, and K(1/2)'s for Ca2+ were between 3 and 5 microM. No binding to the intracellular loops was observed. Binding competition experiments with synthetic peptides mapped the calmodulin binding site to a 10-30 amino acid segment at the beginning of the C-terminal domain of Cx36. The micromolar K(1/2)'s and rapid on and off rates suggest that this interaction may change dynamically in neurons, and may occur transiently when Ca2+ is elevated to a level that would occur in the near vicinity of an activated synapse.

journal_name

Biochem Biophys Res Commun

journal_title

Biochemical and biophysical research communications

authors

Burr GS,Mitchell CK,Keflemariam YJ,Heidelberger R,O'Brien J

doi

10.1016/j.bbrc.2005.08.007

subject

Has Abstract

pub_date

2005-10-07 00:00:00

pages

1191-8

issue

4

eissn

0006-291X

issn

1090-2104

pii

S0006-291X(05)01678-5

journal_volume

335

pub_type

杂志文章

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