'Information storage in the nervous system requires transcription triggered by synaptically evoked calcium signals. It has been suggested that translocation of calmodulin into the nucleus, initiated by submembranous calcium transients, relays synaptic signals to CREB. Here we show that in hippocampal neurons, signaling to CREB can be activated by nuclear ... More
Free and bound intracellular calmodulin measurements in cardiac myocytes.
AuthorsWu X, Bers DM
JournalCell Calcium
PubMed ID16999996
'Calmodulin (CaM) is a ubiquitous Ca2+ binding protein and Ca2+-CaM activates many cellular targets and functions. While much of CaM is thought to be protein bound, quantitative data in cardiac myocytes is lacking regarding CaM location, [CaM]free and CaM redistribution during changes in [Ca2+]i. Here, we demonstrated that in adult ... More
Calcium-dependent association of calmodulin with the C-terminal domain of the tetraspanin protein peripherin/rds.
AuthorsEdrington TC, Yeagle PL, Gretzula CL, Boesze-Battaglia K
JournalBiochemistry
PubMed ID17323925
'Peripherin/rds (p/rds), an integral membrane protein from the transmembrane 4 (TMF4) superfamily, possesses a multi-functional C-terminal domain that plays crucial roles in rod outer segment (ROS) disk renewal and structure. Here, we report that the calcium binding protein calmodulin (CaM) binds to the C-terminal domain of p/rds. Fluorescence spectroscopy reveals ... More
Calcium ion fluorescence detection using liposomes containing Alexa-labeled calmodulin.
AuthorsNguyen T, Rosenzweig Z
JournalAnal Bioanal Chem
PubMed ID12207244
'This paper describes the preparation and characterization of calcium ion sensitive fluorescent liposomes and their application for the determination of calcium ions in aqueous samples. Calmodulin (CaM), a calcium ion-binding protein labeled with the fluorophore Alexa-488 is embedded in the membrane of unilamellar liposomes. Upon calcium ion binding, calmodulin undergoes ... More
A calmodulin binding domain of RyR increases activation of spontaneous Ca2+ sparks in frog skeletal muscle.
AuthorsRodney GG, Wilson GM, Schneider MF
JournalJ Biol Chem
PubMed ID15640144
The calmodulin C lobe binding region (residues 3614-3643) on the sarcoplasmic reticulum Ca2+ release channel (RyR1) is thought to be a region of contact between subunits within RyR1 homotetramer Ca2+ release channels. To determine whether the 3614-3643 region is a regulatory site/interaction domain within RyR in muscle fibers, we have ... More