Conformational regulation and target-myristoyl switch of calcineurin B homologous protein 3.

ABSTRACT: Calcineurin B homologous protein 3 (CHP3) is an EF-hand Ca²⁺-binding protein involved in regulation of cancerogenesis, cardiac hypertrophy, and neuronal development through interactions with sodium/proton exchangers (NHEs) and signalling proteins. While the importance of Ca²⁺ binding and myristoylation for CHP3 function has been recognized, the underlying molecular mechanism remained elusive. In this study, we demonstrate that Ca²⁺ binding and myristoylation independently affect the conformation and functions of human CHP3. Ca²⁺ binding increased local flexibility and hydrophobicity of CHP3 indicative of an open conformation. The Ca²⁺-bound CHP3 exhibited a higher affinity for NHE1 and associated stronger with lipid membranes compared

SUBMITTER: Becker F 

PROVIDER: S-EPMC10368425 | biostudies-literature | 2023 Jul

REPOSITORIES: biostudies-literature