S100A6 is a positive regulator of PPP5C-FKBP51-dependent regulation of endothelial calcium signaling.

ABSTRACT: I_SOC is a cation current permeating the ISOC channel. In pulmonary endothelial cells, I_SOC activation leads to formation of inter-endothelial cell gaps and barrier disruption. The immunophilin FK506-binding protein 51 (FKBP51), in conjunction with the serine/threonine protein phosphatase 5C (PPP5C), inhibits I_SOC . Free PPP5C assumes an autoinhibitory state, which has low "basal" catalytic activity. Several S100 protein family members bind PPP5C increasing PPP5C catalytic activity in vitro. One of these family members, S100A6, exhibits a calcium-dependent translocation to the plasma membrane. The goal of this study was to determine whether S100A6 activates PPP5C in pulmonary endothelial cells and contributes to I_SOC inhibition by the PPP5C-FKBP51

SUBMITTER: Haldar B 

PROVIDER: S-EPMC7401177 | biostudies-literature | 2020 Feb

REPOSITORIES: biostudies-literature