期刊
FEBS JOURNAL
卷 279, 期 8, 页码 1414-1421出版社
WILEY-BLACKWELL
DOI: 10.1111/j.1742-4658.2012.08560.x
关键词
calpain; ESCRT; evolution; microtubule-interacting and transport (MIT); penta-EF-hand
资金
- Ministry of Education, Culture, Sports, Science and Technology (MEXT) [19044017, 21025014]
- [21-6274]
- Grants-in-Aid for Scientific Research [19044017, 21025014, 09J06274] Funding Source: KAKEN
The name calpain was historically given to a protease that is activated by Ca2+ and whose primary structure contains a Ca2+-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 Ca2+-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 proteinprotein interaction networks imply that there is an evolutionary and physical linkage between mammalian calpains and PEF proteins involving the ESCRT system.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据