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Evolutionary and physical linkage between calpains and penta‐EF‐hand Ca 2+ ‐binding proteins
Author(s) -
Maki Masatoshi,
Maemoto Yuki,
Osako Yohei,
Shibata Hideki
Publication year - 2012
Publication title -
the febs journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.981
H-Index - 204
eISSN - 1742-4658
pISSN - 1742-464X
DOI - 10.1111/j.1742-4658.2012.08560.x
Subject(s) - escrt , calpain , protein subunit , protein domain , microbiology and biotechnology , tsg101 , endosome , biology , gene , transport protein , genetics , biochemistry , enzyme , microrna , microvesicles , intracellular
The name calpain was historically given to a protease that is activated by Ca 2+ and whose primary structure contains a Ca 2+ ‐binding penta‐EF‐hand (PEF) as well as a calpain cysteine protease (CysPc) domain and a C2‐domain‐like (C2L) domain. In the human genome, CysPc domains are found in 15 genes, but only nine of them encode PEF domains. Fungi and budding yeasts have calpain‐like sequences that lack the PEF domain, and each protein (designated PalB and Rim13, respectively) is orthologous to human calpain‐7, indicating that the calpain‐7 orthologs are evolutionarily more conserved than classical calpains possessing PEF domains. An N‐terminal region of calpain‐7 has a tandem repeat of microtubule‐interacting and transport domains that interact with a subset of endosomal sorting complex required for transport (ESCRT) III proteins. In addition to calpains, PEF domains are found in other Ca 2+ ‐binding proteins including ALG‐2 that associates with ALIX (an ESCRT‐III accessory protein) and TSG101 (an ESCRT‐I subunit). Phylogenetic comparison of dissected domain structures of calpains and experimentally confirmed protein–protein interaction networks imply that there is an evolutionary and physical linkage between mammalian calpains and PEF proteins involving the ESCRT system.