S92 phosphorylation induces structural changes in the N-terminus domain of human mitochondrial calcium uniporter.

ABSTRACT: The mitochondrial calcium uniporter (MCU) plays essential roles in mitochondrial calcium homeostasis and regulates cellular functions, such as energy synthesis, cell growth, and development. Thus, MCU activity is tightly controlled by its regulators as well as post-translational modification, including phosphorylation by protein kinases such as proline-rich tyrosine kinase 2 (Pyk2) and AMP-activated protein kinase (AMPK). In our in vitro kinase assay, the MCU N-terminal domain (NTD) was phosphorylated by protein kinase C isoforms (PKC_βII, PKC_δ, and PKC_ε) localized in the mitochondrial matrix. In addition, we found the conserved S92 was phosphorylated by the PKC isoforms. To reveal the structural effect of MCU S92 phosphorylation (S92p), we determined crysta

SUBMITTER: Lee Y 

PROVIDER: S-EPMC7272466 | biostudies-literature | 2020 Jun

REPOSITORIES: biostudies-literature