Historical Background
The entry of the calcium ion into the cytoplasm of cells from the extracellular medium or from intracellular stores plays an important signaling role. Cytoplasmic calcium acts as a signal by binding to high-affinity calcium-binding proteins. These proteins in turn act as transducers of the signal by activating other proteins or may be activated directly to carry out enzymatic or structural changes. In this way, many extracellular signals are converted into intracellular activities.
An important subset of these intracellular calcium-binding proteins are proteins that also interact with membranes in a calcium-regulated fashion. In the resting cell, many of these proteins are freely soluble in the cytoplasm (or nucleoplasm). However, when calcium enters the cell, these proteins move onto membrane surfaces. In this way, they make fundamental changes in the character of the membrane surface. Some, such as the annexins (Gerke et al. 2005), are so abundant that up to...
This is a preview of subscription content, log in via an institution to check access.
Access this chapter
Tax calculation will be finalised at checkout
Purchases are for personal use only
References
Caudell EG, Caudell JJ, Tang CH, Yu TK, Frederick MJ, Grimm EA. Characterization of human copine III as a phosphoprotein with associated kinase activity. Biochemistry. 2000;39:13034–43.
Church DL, Lambie EJ. The promotion of gonadal dell divisions by the Caenorhabditis elegans TRPM cation channel GON-2 is antagonized by GEM-4 copine. Genetics. 2003;165:563–74.
Creutz CE, Hira JK, Gee VE, Eaton JM. Protection of the membrane permeability barrier by annexins. Biochemistry. 2012;51:9966–83.
Creutz CE, Tomsig JL, Snyder SL, Skouri F, Beisson J, Cohen J. The copines: a novel class of C2 domain-containing, calcium-dependent, phospholipid-binding proteins conserved from Paramecium to humans. J Biol Chem. 1998;273:1393–402.
Damer CK, Bayeva M, Hahn ES, Rivera J, Socec CI. Copine A, a calcium-dependent membrane-binding protein, transiently localizes to the plasma membrane and intracellular vacuoles in Dictyostelium. BMC Cell Biol. 2005;6:46.
Damer CK, Bayeva M, Kim PS, Ho LK, Eberhardt ES, Socec CI, Lee LS, Bruce EA, Goldman-Yassen AE, Naliboff LC. Copine A is required for cytokinesis, contractile vacuole function, and development in Dictyostelium. Eukaryot Cell. 2007;6:430–42.
Emsley J, Knight CG, Farndale RW, Barnes MJ, Liddington RC. Structural basis of collagen recognition by integrin alpha2beta1. Cell. 2000;101:47–56.
Gerke V, Creutz CE, Moss SE. Annexins: linking Ca2+ signalling to membrane dynamics. Nat Rev Mol Cell Biol. 2005;6:449–61.
Gottschalk A, Almedom RB, Schedletzky T, Anderson SD, Yates JR, Schafer WR. Identification and characterization of novel nicotinic receptor-associated proteins in Caenorhabditis elegans. EMBO J. 2005;24:2566–78.
Heinrich C, Keller C, Boulay A, Vecchi M, Bianchi M, Sack R, Lienhard S, Duss S, Hofsteenge J, Hynes NE. Copine-III interacts with ErbB2 and promotes tumor cell migration. Oncogene. 2010;29:1598–610.
Hua J, Grisafi P, Cheng SH, Fink GR. Plant growth homeostasis is controlled by the Arabidopsis BON1 and BAP1 genes. Genes Dev. 2001;15:2263–72.
Jambunathan N, Siani JM, McNellis TW. A humidity-sensitive Arabidopsis copine mutant exhibits precocious cell death and increased disease resistance. Plant Cell. 2001;13:2225–40.
Lee JO, Rieu P, Arnaout MA, Liddington R. Crystal structure of the A domain from the alpha subunit of integrin CR3 (CD11b/CD18). Cell. 1995;80:631–8.
Nakayama T, Yaoi T, Yasui M, Kuwajima G. N-copine: a novel two C2-domain-containing protein with neuronal activity-regulated expression. FEBS Lett. 1998;428:80–4.
Reinhard JR, Kriz A, Galic M, Angliker N, Rajalu M, Vogt KE, Ruegg MA. The calcium sensor copine-6 regulates spine structural plasticity and learning and memory. Nat Commun. 2016;7:11613. https://doi.org/10.1038/ncomms11613.
Tomsig JL, Creutz CE. Biochemical characterization of copine: a ubiquitous calcium-dependent, phospholipid-binding protein. Biochemistry. 2000;39:16163–75.
Tomsig JL, Creutz CE. Copines: a ubiquitous family of Calcium-dependent, phospholipid-binding proteins. Cell Mol Life Sci. 2002;59:1467–77.
Tomsig JL, Snyder SL, Creutz CE. Identification of targets for calcium signalling through the copine family of proteins. Characterization of a coiled-coil copine-binding motif. J Biol Chem. 2003;278:10048–54.
Tomsig JL, Sohma H, Creutz CE. Calcium-dependent regulation of tumour necrosis factor-alpha receptor signalling by copine. Biochem J. 2004;378:1089–94.
Author information
Authors and Affiliations
Corresponding author
Editor information
Editors and Affiliations
Copyright information
© 2018 Springer International Publishing AG
About this entry
Cite this entry
Creutz, C.E. (2018). Copine. In: Choi, S. (eds) Encyclopedia of Signaling Molecules. Springer, Cham. https://doi.org/10.1007/978-3-319-67199-4_56
Download citation
DOI: https://doi.org/10.1007/978-3-319-67199-4_56
Published:
Publisher Name: Springer, Cham
Print ISBN: 978-3-319-67198-7
Online ISBN: 978-3-319-67199-4
eBook Packages: Biomedical and Life SciencesReference Module Biomedical and Life Sciences