Ontology highlight
ABSTRACT:
SUBMITTER: Montgomery DS
PROVIDER: S-EPMC5538800 | biostudies-literature | 2017 Jul
REPOSITORIES: biostudies-literature
Montgomery Darrice S DS Yu Ling L Ghazi Zinah M ZM Thai Tiffany L TL Al-Khalili Otor O Ma He-Ping HP Eaton Douglas C DC Alli Abdel A AA
American journal of physiology. Cell physiology 20170503 1
We previously demonstrated a role for the myristoylated alanine-rich C kinase substrate (MARCKS) to serve as an adaptor protein in the anionic phospholipid phosphate-dependent regulation of the epithelial sodium channel (ENaC). Both MARCKS and ENaC are regulated by proteolysis. Calpains are a family of ubiquitously expressed intracellular Ca<sup>2+</sup>-dependent cysteine proteases involved in signal transduction. Here we examine the role of calpain-2 in regulating MARCKS and ENaC in cultured r ...[more]