Abstract

Neurocalcin is an N-myristoylated calcium-binding protein which belongs to a novel family of neuronal calcium sensors. Here we show, by cosedimentation, co-immunoprecipitation and cross-linking approaches, that myristoylated neurocalcin directly interacts with actin in a calcium-dependent manner. We used EDC cross-linking and obtained one novel 64 kDa entity composed of one actin molecule and one neurocalcin molecule, as demonstrated with IAEDANS-actin and neurocalcin-specific antibodies. This interaction could modulate the rod outer segment-guanylate cyclase 1-neurocalcin interface.

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