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Article

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

Biochimica et biophysica acta. Molecular cell research - 1 Jun 2021

Bondada Vimala, Gal Jozsef, Mashburn Charles, Rodgers David W, Larochelle Katherine E, Croall Dorothy E, Geddes James W

Abstract excerpt

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...

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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Identifiers

PMID: 33811937
DOI: 10.1016/j.bbamcr.2021.119019
PMCID: PMC8588747

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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