The world's first wiki where authorship really matters (Nature Genetics, 2008). Due credit and reputation for authors. Imagine a global collaborative knowledge base for original thoughts. Search thousands of articles and collaborate with scientists around the globe.

wikigene or wiki gene protein drug chemical gene disease author authorship tracking collaborative publishing evolutionary knowledge reputation system wiki2.0 global collaboration genes proteins drugs chemicals diseases compound
Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)



Gene Review

Canx  -  calnexin

Rattus norvegicus

Synonyms: Calnexin
Welcome! If you are familiar with the subject of this article, you can contribute to this open access knowledge base by deleting incorrect information, restructuring or completely rewriting any text. Read more.

High impact information on Canx

  • Autocrine motility factor receptor (AMF-R) is a marker for a smooth subdomain of the ER, shown here by confocal microscopy to be distinct from, yet closely associated with the calnexin- or calreticulin-labeled ER [1].
  • This is deduced from the effect of antibodies to the COOH-terminal tail of alpha(2)p24, but not of antibodies to the COOH-terminal tail of calnexin on this reconstitution, as well as the demonstrated recruitment of COPI coatomer to VTCs, its augmentation by GTPgammaS, inhibition by Brefeldin A (BFA), or depletion of beta-COP from cytosol [2].
  • Taken together with studies revealing calnexin association with CK2 and ERK-1, a model is proposed whereby phosphorylation of calnexin leads to a potential increase in glycoprotein folding close to the translocon [3].
  • Phosphorylation by CK2 and MAPK enhances calnexin association with ribosomes [3].
  • Remarkably, DLP1-positive structures coalign with microtubules and, most strikingly, with endoplasmic reticulum tubules as verified by double labeling with antibodies to calnexin and Rab1 as well as by immunoelectron microscopy [4].

Biological context of Canx

  • Partial amino acid sequence analysis revealed that p93 was close to 100% homologous with a recently identified ER Ca(2+)-binding protein known as calnexin [5].
  • Using truncated RNA templates we found that calnexin did not associate with the first four TM domains but retained affinity for the construct encoding TM domains 5 and 6, which contains the glycosylation sites [6].
  • Stable transfection of FR3T3 rat fibroblast cells with p79 cDNA analysed by electron microscopy following immunolabelling of ultra-thin cryosections revealed a localization of p79 in the secretory pathway, mainly in the endoplasmic reticulum and the Golgi region, where it is specifically associated with the molecular chaperone calnexin [7].

Anatomical context of Canx


Associations of Canx with chemical compounds

  • A subset of these luminal components are specific for glycoproteins, and, like calnexin and calreticulin, the thiol-dependent reductase ERp57 has been shown to interact specifically with soluble secretory proteins bearing N-linked carbohydrate [8].
  • Biosynthesis of inositol trisphosphate receptors: selective association with the molecular chaperone calnexin [6].
  • Glucose trimming from newly synthesized glycoproteins regulates their interaction with the calnexin/calreticulin chaperone system [11].
  • The interaction of calnexin with newly synthesized type-I IP(3)R was transient and inhibited by treatment of the cells with dithiothreitol or the glucosidase inhibitor N-methyldeoxynojirimicin [6].

Other interactions of Canx


  1. Calcium regulates the association between mitochondria and a smooth subdomain of the endoplasmic reticulum. Wang, H.J., Guay, G., Pogan, L., Sauvé, R., Nabi, I.R. J. Cell Biol. (2000) [Pubmed]
  2. Roles for alpha(2)p24 and COPI in endoplasmic reticulum cargo exit site formation. Lavoie, C., Paiement, J., Dominguez, M., Roy, L., Dahan, S., Gushue, J.N., Bergeron, J.J. J. Cell Biol. (1999) [Pubmed]
  3. Phosphorylation by CK2 and MAPK enhances calnexin association with ribosomes. Chevet, E., Wong, H.N., Gerber, D., Cochet, C., Fazel, A., Cameron, P.H., Gushue, J.N., Thomas, D.Y., Bergeron, J.J. EMBO J. (1999) [Pubmed]
  4. A novel dynamin-like protein associates with cytoplasmic vesicles and tubules of the endoplasmic reticulum in mammalian cells. Yoon, Y., Pitts, K.R., Dahan, S., McNiven, M.A. J. Cell Biol. (1998) [Pubmed]
  5. Identification and purification of a calcium-binding protein in hepatic nuclear membranes. Gilchrist, J.S., Pierce, G.N. J. Biol. Chem. (1993) [Pubmed]
  6. Biosynthesis of inositol trisphosphate receptors: selective association with the molecular chaperone calnexin. Joseph, S.K., Boehning, D., Bokkala, S., Watkins, R., Widjaja, J. Biochem. J. (1999) [Pubmed]
  7. Identification and characterization of an intracellular protein complex that binds fibroblast growth factor-2 in bovine brain. Chevet, E., Lemaître, G., Cailleret, K., Dahan, S., Bergeron, J.J., Katinka, M.D. Biochem. J. (1999) [Pubmed]
  8. The thiol-dependent reductase ERp57 interacts specifically with N-glycosylated integral membrane proteins. Elliott, J.G., Oliver, J.D., High, S. J. Biol. Chem. (1997) [Pubmed]
  9. Isolation of subcellular agonist-sensitive calcium stores from the pancreatic acinar cell. Pandol, S.J., Fitzsimmons, T., Schoeffield-Payne, M., Carlile, G.W., Evans, W.H. Cell Calcium (1995) [Pubmed]
  10. Characterization and comparison of raft-like membranes isolated by two different methods from rat submandibular gland cells. García-Marcos, M., Pochet, S., Tandel, S., Fontanils, U., Astigarraga, E., Fernández-González, J.A., Kumps, A., Marino, A., Dehaye, J.P. Biochim. Biophys. Acta (2006) [Pubmed]
  11. Quaternary and domain structure of glycoprotein processing glucosidase II. Trombetta, E.S., Fleming, K.G., Helenius, A. Biochemistry (2001) [Pubmed]
  12. NMR structures of 36 and 73-residue fragments of the calreticulin P-domain. Ellgaard, L., Bettendorff, P., Braun, D., Herrmann, T., Fiorito, F., Jelesarov, I., Güntert, P., Helenius, A., Wüthrich, K. J. Mol. Biol. (2002) [Pubmed]
  13. Distribution of inositol 1,4,5-trisphosphate receptor isoforms, SERCA isoforms and Ca2+ binding proteins in RBL-2H3 rat basophilic leukemia cells. Vanlingen, S., Parys, J.B., Missiaen, L., De Smedt, H., Wuytack, F., Casteels, R. Cell Calcium (1997) [Pubmed]
  14. The organization of the endoplasmic reticulum and the intermediate compartment in cultured rat hippocampal neurons. Krijnse-Locker, J., Parton, R.G., Fuller, S.D., Griffiths, G., Dotti, C.G. Mol. Biol. Cell (1995) [Pubmed]
  15. Intracellular Ca2+ stores of rat cerebellum: heterogeneity within and distinction from endoplasmic reticulum. Nori, A., Villa, A., Podini, P., Witcher, D.R., Volpe, P. Biochem. J. (1993) [Pubmed]
WikiGenes - Universities