Ontology highlight
ABSTRACT: Rationale
Trimeric intracellular cation (TRIC)-A and B are distributed to endoplasmic reticulum/sarcoplasmic reticulum intracellular Ca2+ stores. The crystal structure of TRIC has been determined, confirming the homotrimeric structure of a potassium channel. While the pore architectures of TRIC-A and TRIC-B are conserved, the carboxyl-terminal tail (CTT) domains of TRIC-A and TRIC-B are different from each other. Aside from its recognized role as a counterion channel that participates in excitation-contraction coupling of striated muscles, the physiological function of TRIC-A in heart physiology and disease has remained largely unexplored.Objective
In cardiomyocytes, spontaneous Ca2+ waves, triggered by store overload-induced Ca2+ release me
SUBMITTER: Zhou X
PROVIDER: S-EPMC7035183 | biostudies-literature | 2020 Feb
REPOSITORIES: biostudies-literature