Loop 2 of limulus myosin III is phosphorylated by protein kinase A and autophosphorylation.

ABSTRACT: Little is known about the functions of class III unconventional myosins although, with an N-terminal kinase domain, they are potentially both signaling and motor proteins. Limulus myosin III is particularly interesting because it is a phosphoprotein abundant in photoreceptors that becomes more heavily phosphorylated at night by protein kinase A. This enhanced nighttime phosphorylation occurs in response to signals from an endogenous circadian clock and correlates with dramatic changes in photoreceptor structure and function. We seek to understand the role of Limulus myosin III and its phosphorylation in photoreceptors. Here we determined the sites that become phosphorylated in Limulus myosin III and investigated its kinase, actin binding, and myosin ATPase activities. We show that Limulus

SUBMITTER: Kempler K 

PROVIDER: S-EPMC2580675 | biostudies-literature | 2007 Apr

REPOSITORIES: biostudies-literature