Ontology highlight
ABSTRACT:
SUBMITTER: Lin YC
PROVIDER: S-EPMC2867382 | biostudies-literature | 2010 May
REPOSITORIES: biostudies-literature
Lin Yen-Chang YC Huang Jianying J Zhang Qi Q Hollander John M JM Frisbee Jefferson C JC Martin Karen H KH Nestor Casey C Goodman Robert R Yu Han-Gang HG
American journal of physiology. Cell physiology 20100217 5
Ca(2+) entry is delicately controlled by inactivation of L-type calcium channel (LTCC) composed of the pore-forming subunit alpha1C and the auxiliary subunits beta1 and alpha2delta. Calmodulin is the key protein that interacts with the COOH-terminal motifs of alpha1C, leading to the fine control of LTCC inactivation. In this study we show evidence that a hyperpolarization-activated cyclic nucleotide-gated channel, HCN2, can act as a nonchannel regulatory protein to narrow the L-type Ca(2+) chann ...[more]