The C2 domain of calpain 5 contributes to enzyme activation and membrane localization.

ABSTRACT: The enzymatic characteristics of the ubiquitous calpain 5 (CAPN5) remain undescribed despite its high expression in the central nervous system and links to eye development and disease. CAPN5 contains the typical protease core domains but lacks the C terminal penta-EF hand domain of classical calpains, and instead contains a putative C2 domain. This study used the SH-SY5Y neuroblastoma cell line stably transfected with CAPN5-3xFLAG variants to assess the potential roles of the CAPN5 C2 domain in Ca²⁺ regulated enzyme activity and intracellular localization. Calcium dependent autoproteolysis of CAPN5 was documented and characterized. Mutation of the catalytic Cys81 to Ala or addition of EGTA prevented autolysis. Eighty μM Ca²⁺ was sufficient to stimulate half-maximal CA

SUBMITTER: Bondada V 

PROVIDER: S-EPMC8588747 | biostudies-literature | 2021 Jun

REPOSITORIES: biostudies-literature