Calcium-binding proteins: Intracellular sensors from the calmodulin superfamily

被引:131
作者
Haeseleer, F
Imanishi, Y
Sokal, I
Filipek, S
Palczewski, K
机构
[1] Univ Washington, Dept Ophthalmol, Seattle, WA 98195 USA
[2] Univ Washington, Dept Chem, Seattle, WA 98195 USA
[3] Univ Washington, Dept Pharmacol, Seattle, WA 98195 USA
[4] Univ Warsaw, Dept Chem, PL-02093 Warsaw, Poland
关键词
D O I
10.1006/bbrc.2001.6228
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
In all eukaryotic cells, and particularly in neurons, Ca2+ ions are important second messengers in a variety of cellular signaling pathways. In the retina, Ca2+ modulation plays a crucial function in the development of the visual system's neuronal connectivity and a regulatory role in the conversion of the light signal received by photoreceptors into an electrical signal transmitted to the brain. Therefore, the study of retinal Ca2+-binding proteins, which frequently mediate Ca2+ signaling, has given rise to the important discovery of two subfamilies of these proteins, neuronal Ca2+-binding proteins (NCBPs) and calcium-binding proteins (CaBPs), that display similarities to calmodulin (CaM). These and other Ca2+-binding proteins are integral components of cellular events controlled by Ca2+. Some members of these subfamilies also play a vital role in signal transduction outside of the retina. The expansion of the CaM-like protein family reveals diversification among Ca2+-binding proteins that evolved on the basis of the classic molecule, CaM. A large number of NCBP and CaBP subfamily members would benefit from their potentially specialized role in Ca2+-dependent cellular processes. Pinpointing the role of these proteins will be a challenging task for further research. (C) 2002 Elsevier Science.
引用
收藏
页码:615 / 623
页数:9
相关论文
共 79 条
[1]   An open and shut case [J].
Akke, M ;
Chazin, WJ .
NATURE STRUCTURAL BIOLOGY, 2001, 8 (11) :910-912
[2]  
Ames JB, 2000, METHOD ENZYMOL, V316, P121
[3]   Structure and calcium-binding properties of Frq1, a novel calcium sensor in the yeast Saccharomyces cerevisiae [J].
Ames, JB ;
Hendricks, KB ;
Strahl, T ;
Huttner, IG ;
Hamasaki, N ;
Thorner, J .
BIOCHEMISTRY, 2000, 39 (40) :12149-12161
[4]   Modulation of A-type potassium channels by a family of calcium sensors [J].
An, WF ;
Bowlby, MR ;
Betty, M ;
Cao, J ;
Ling, HP ;
Mendoza, G ;
Hinson, JW ;
Mattsson, KI ;
Strassle, BW ;
Trimmer, JS ;
Rhodes, KJ .
NATURE, 2000, 403 (6769) :553-556
[5]   3-DIMENSIONAL STRUCTURE OF CALMODULIN [J].
BABU, YS ;
SACK, JS ;
GREENHOUGH, TJ ;
BUGG, CE ;
MEANS, AR ;
COOK, WJ .
NATURE, 1985, 315 (6014) :37-40
[6]   COMPREHENSIVE EXAMINATION OF PROTEIN SEQUENCES FOR EVIDENCE OF INTERNAL GENE DUPLICATION [J].
BARKER, WC ;
KETCHAM, LK ;
DAYHOFF, MO .
JOURNAL OF MOLECULAR EVOLUTION, 1978, 10 (04) :265-281
[7]  
Boekhoff I, 1997, EUR J CELL BIOL, V72, P151
[8]   Immunocytochemical localization and crystal structure of human frequenin (neuronal calcium sensor 1) [J].
Bourne, Y ;
Dannenberg, J ;
Pollmann, V ;
Marchot, P ;
Pongs, O .
JOURNAL OF BIOLOGICAL CHEMISTRY, 2001, 276 (15) :11949-11955
[9]  
Boycott B, 1999, INVEST OPHTH VIS SCI, V40, P1313
[10]  
Braunewell KH, 1997, J NEUROCHEM, V68, P2129