Structures, functions and molecular evolution of the penta-EF-hand Ca2+-binding proteins

被引：147

作者：

Maki, M ^{[1
]}

Kitaura, Y ^{[1
]}

Satoh, H ^{[1
]}

Ohkouchi, S ^{[1
]}

Shibata, H ^{[1
]}

机构：

[1] Nagoya Univ, Lab Mol & Cellular Regulat, Dept Appl Mol Biosci, Grad Sch Bioagr Sci,Chikusa Ku, Nagoya, Aichi 4648601, Japan

来源：

BIOCHIMICA ET BIOPHYSICA ACTA-PROTEINS AND PROTEOMICS | 2002年 / 1600卷 / 1-2期

关键词：

penta-EF-hand; Ca2+-binding protein; ALG-2; peflin; sorcin; calpain;

D O I：

10.1016/S1570-9639(02)00444-2

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Penta-EF-hand (PEF) proteins comprise a family of Ca2+-binding proteins that have five repetitive EF-hand motifs. Among the eight alpha-helices (alpha1-alpha8), alpha4 and alpha7 link EF2-EIF3 and EF4-EF5, respectively. In addition to the structural similarities in the EF-hand regions, the PEF protein family members have common features: (i) dimerization through unpaired C-terminal EF5s, (ii) possession of hydrophobic Gly/ Pro-rich N-terminal domains, and (.)(iii) Ca2+-dependent translocation to membranes. Based on comparison of amino acid sequences, mammalian PEF proteins are classified into two groups: Group I PEF proteins (ALG-2 and peflin) and Group II PEF proteins (Ca2+- dependent protease calpain subfamily members, sorcin and grancalcin). The Group I genes have also been found in lower animals, plants, fungi and protists. Recent findings of specific interacting proteins have started to gradually unveil the functions of the noncatalytic mammalian PEF proteins. (C) 2002 Elsevier Science B.V. All fights reserved.

引用

页码：51 / 60

页数：10

共 87 条

[1] Disruption of the murine calpain small subunit gene, Capn4:: Calpain is essential for embryonic development but not for cell growth and division [J].