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07:51
Pull-down of Calmodulin-binding Proteins
Published on: January 23, 2012
Evolutionary and physical linkage between calpains and penta-EF-hand Ca2+-binding proteins
Masatoshi Maki1, Yuki Maemoto, Yohei Osako
1Department of Applied Molecular Biosciences, Graduate School of Bioagricultural Sciences, Nagoya University, Chikusa-ku, Nagoya, Japan. mmaki@agr.nagoya-u.ac.jp
The FEBS Journal
|March 13, 2012
Summary
Calpains are Ca(2+)-activated proteases. Evolutionary analysis reveals conserved calpain-7 orthologs in fungi and yeasts, linked to the ESCRT system via PEF domains.
Area of Science:
- Molecular Biology
- Evolutionary Biology
- Biochemistry
Background:
- Calpains are Ca(2+)-activated proteases characterized by penta-EF-hand (PEF), calpain cysteine protease (CysPc), and C2-domain-like (C2L) domains.
- Human genomes contain 15 CysPc domain genes, with nine encoding PEF domains, defining classical calpains.
Purpose of the Study:
- To investigate the evolutionary conservation and functional relationships of calpain-like proteins and PEF domain-containing proteins.
- To explore the involvement of the endosomal sorting complex required for transport (ESCRT) system in calpain-mediated pathways.
Main Methods:
- Phylogenetic analysis of calpain and PEF domain structures across species.
- Examination of protein-protein interaction networks, including interactions with ESCRT components.
Main Results:
- Calpain-7 orthologs in fungi and yeasts lack PEF domains, suggesting greater evolutionary conservation than classical calpains.
- Calpain-7 interacts with ESCRT-III proteins via its N-terminal microtubule-interacting and transport domains.
- PEF domains are also found in Ca(2+)-binding proteins like ALG-2, which associate with ESCRT proteins (ALIX, TSG101).
Conclusions:
- There is an evolutionary and physical link between mammalian calpains and PEF proteins, mediated by the ESCRT system.
- This linkage highlights a conserved mechanism involving Ca(2+)-binding proteins and the ESCRT machinery across different species.
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