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CANX  -  calnexin

Canis lupus familiaris

 
 
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Disease relevance of CANX

 

High impact information on CANX

 

Biological context of CANX

 

Anatomical context of CANX

  • Calnexin and ERp57 act cooperatively to ensure a proper folding of proteins in the endoplasmic reticulum (ER) [8].
  • Protease protection experiments with intact canine rough microsomes showed that amino acid residues 1-462 of calnexin are located within the lumen of the endoplasmic reticulum [1].
  • To determine their role in the maturation of newly synthesized glycoproteins, we analyzed the folding and trimerization of in vitro translated influenza hemagglutinin (HA) in canine pancreas microsomes under conditions in which HA's interactions with CNX and CRT could be manipulated [9].
  • Calnexin fails to associate with substrate proteins in glucosidase-deficient cell lines [10].
  • Here we describe that the lumenal surface of the ER membranes transiently tethers the folding intermediate of secretory proteins via a 90-kDa ER membrane protein, calnexin [11].
 

Associations of CANX with chemical compounds

  • Our results identify the luminal domain of calnexin as responsible for binding substrates, Ca2+, and Mg-ATP [1].
  • Triton X-114 partitioning of the integral membrane proteins of rough microsomes suggested that pgp35 (SSR alpha) and calnexin were major Ca(2+)-binding proteins of the endoplasmic reticulum membrane [12].
  • We demonstrate that the properties of the purified calnexin delta TMC correspond to those of full-length calnexin in canine microsomes with at least one intramolecular disulfide bond and binding to 45Ca2+ [1].
  • If HA's binding to CNX and CRT was inhibited using a glucosidase inhibitor, castanospermine (CST), the rate of disulfide formation and oligomerization was doubled but the overall efficiency of maturation of HA decreased due to aggregation and degradation [9].
  • Perturbation of the redox state by 5 mM dithiothreitol or 1 mM diamide markedly inhibited the dissociation of p70 from calnexin (t1/2 > 30 min) [11].
 

Analytical, diagnostic and therapeutic context of CANX

References

  1. Conformational changes induced in the endoplasmic reticulum luminal domain of calnexin by Mg-ATP and Ca2+. Ou, W.J., Bergeron, J.J., Li, Y., Kang, C.Y., Thomas, D.Y. J. Biol. Chem. (1995) [Pubmed]
  2. Glucose trimming and reglucosylation determine glycoprotein association with calnexin in the endoplasmic reticulum. Hebert, D.N., Foellmer, B., Helenius, A. Cell (1995) [Pubmed]
  3. N-linked glycans direct the cotranslational folding pathway of influenza hemagglutinin. Daniels, R., Kurowski, B., Johnson, A.E., Hebert, D.N. Mol. Cell (2003) [Pubmed]
  4. 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]
  5. Primary structure and characterization of an Arabidopsis thaliana calnexin-like protein. Huang, L., Franklin, A.E., Hoffman, N.E. J. Biol. Chem. (1993) [Pubmed]
  6. Molecular cloning of a novel Ca(2+)-binding protein (calmegin) specifically expressed during male meiotic germ cell development. Watanabe, D., Yamada, K., Nishina, Y., Tajima, Y., Koshimizu, U., Nagata, A., Nishimune, Y. J. Biol. Chem. (1994) [Pubmed]
  7. cDNA-based functional domains of a calnexin-like melanosomal protein, p90. Vinayagamoorthy, T., Dakour, J., Dixon, W., Jimbow, K. Melanoma Res. (1993) [Pubmed]
  8. Specific interaction of ERp57 and calnexin determined by NMR spectroscopy and an ER two-hybrid system. Pollock, S., Kozlov, G., Pelletier, M.F., Trempe, J.F., Jansen, G., Sitnikov, D., Bergeron, J.J., Gehring, K., Ekiel, I., Thomas, D.Y. EMBO J. (2004) [Pubmed]
  9. Calnexin and calreticulin promote folding, delay oligomerization and suppress degradation of influenza hemagglutinin in microsomes. Hebert, D.N., Foellmer, B., Helenius, A. EMBO J. (1996) [Pubmed]
  10. Calnexin fails to associate with substrate proteins in glucosidase-deficient cell lines. Ora, A., Helenius, A. J. Biol. Chem. (1995) [Pubmed]
  11. Chaperone function of calnexin for the folding intermediate of gp80, the major secretory protein in MDCK cells. Regulation by redox state and ATP. Wada, I., Ou, W.J., Liu, M.C., Scheele, G. J. Biol. Chem. (1994) [Pubmed]
  12. SSR alpha and associated calnexin are major calcium binding proteins of the endoplasmic reticulum membrane. Wada, I., Rindress, D., Cameron, P.H., Ou, W.J., Doherty, J.J., Louvard, D., Bell, A.W., Dignard, D., Thomas, D.Y., Bergeron, J.J. J. Biol. Chem. (1991) [Pubmed]
  13. Purification of a 90-kDa protein (Band VII) from cardiac sarcoplasmic reticulum. Identification as calnexin and localization of casein kinase II phosphorylation sites. Cala, S.E., Ulbright, C., Kelley, J.S., Jones, L.R. J. Biol. Chem. (1993) [Pubmed]
  14. The three alpha 2-adrenergic receptor subtypes achieve basolateral localization in Madin-Darby canine kidney II cells via different targeting mechanisms. Wozniak, M., Limbird, L.E. J. Biol. Chem. (1996) [Pubmed]
  15. Identification and crystallization of a protease-resistant core of calnexin that retains biological activity. Hahn, M., Borisova, S., Schrag, J.D., Tessier, D.C., Zapun, A., Tom, R., Kamen, A.A., Bergeron, J.J., Thomas, D.Y., Cygler, M. J. Struct. Biol. (1998) [Pubmed]
  16. A novel approach for N-glycosylation studies using detergent extracted microsomes. Yuki, H., Hamanaka, R., Shinohara, T., Sakai, K., Watanabe, M. Mol. Cell. Biochem. (2005) [Pubmed]
 
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