CaMKIIbeta binding to stable F-actin in vivo regulates F-actin filament stability.

ABSTRACT: Ca2(+)/calmodulin-dependent protein kinase II (CaMKII) is a serine/threonine kinase that is best known for its role in synaptic plasticity and memory. Multiple roles of CaMKII have been identified in the hippocampus, yet its role in developing neurons is less well understood. We show here that endogenous CaMKIIbeta, but not CaMKIIalpha, localized to prominent F-actin-rich structures at the soma in embryonic cortical neurons. Fluorescence recovery after photobleaching analyses of GFP-CaMKIIbeta binding interactions with F-actin in this CaMKIIalpha-free system indicated CaMKIIbeta binding depended upon a putative F-actin binding domain in the variable region of CaMKIIbeta. Furthermore, CaMKIIalpha decreased CaMKIIbeta binding to F-actin. We examined the interaction of CaMKIIbeta with stable

SUBMITTER: Lin YC 

PROVIDER: S-EPMC2572980 | biostudies-literature | 2008 Oct

REPOSITORIES: biostudies-literature