Encyclopedia of Signaling Molecules

2018 Edition
| Editors: Sangdun Choi

Copine

  • Carl E. Creutz
Reference work entry
DOI: https://doi.org/10.1007/978-3-319-67199-4_56

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...

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References

  1. 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.PubMedCrossRefGoogle Scholar
  2. 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.PubMedPubMedCentralGoogle Scholar
  3. Creutz CE, Hira JK, Gee VE, Eaton JM. Protection of the membrane permeability barrier by annexins. Biochemistry. 2012;51:9966–83.PubMedCrossRefGoogle Scholar
  4. 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.PubMedCrossRefGoogle Scholar
  5. 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.PubMedPubMedCentralCrossRefGoogle Scholar
  6. 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.PubMedPubMedCentralCrossRefGoogle Scholar
  7. Emsley J, Knight CG, Farndale RW, Barnes MJ, Liddington RC. Structural basis of collagen recognition by integrin alpha2beta1. Cell. 2000;101:47–56.PubMedCrossRefGoogle Scholar
  8. Gerke V, Creutz CE, Moss SE. Annexins: linking Ca2+ signalling to membrane dynamics. Nat Rev Mol Cell Biol. 2005;6:449–61.PubMedCrossRefGoogle Scholar
  9. 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.PubMedPubMedCentralCrossRefGoogle Scholar
  10. 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.PubMedCrossRefGoogle Scholar
  11. 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.PubMedPubMedCentralCrossRefGoogle Scholar
  12. 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.PubMedPubMedCentralCrossRefGoogle Scholar
  13. 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.PubMedCrossRefGoogle Scholar
  14. 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.PubMedCrossRefGoogle Scholar
  15. 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.CrossRefPubMedPubMedCentralGoogle Scholar
  16. Tomsig JL, Creutz CE. Biochemical characterization of copine: a ubiquitous calcium-dependent, phospholipid-binding protein. Biochemistry. 2000;39:16163–75.PubMedCrossRefGoogle Scholar
  17. Tomsig JL, Creutz CE. Copines: a ubiquitous family of Calcium-dependent, phospholipid-binding proteins. Cell Mol Life Sci. 2002;59:1467–77.PubMedCrossRefGoogle Scholar
  18. 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.PubMedCrossRefGoogle Scholar
  19. Tomsig JL, Sohma H, Creutz CE. Calcium-dependent regulation of tumour necrosis factor-alpha receptor signalling by copine. Biochem J. 2004;378:1089–94.PubMedPubMedCentralCrossRefGoogle Scholar

Copyright information

© Springer International Publishing AG 2018

Authors and Affiliations

  1. 1.Department of PharmacologyUniversity of VirginiaCharlottesvilleUSA