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Giraldo, A.M.V.; Medus, M.L.; Lebrero, M.G.; Pagano, R.S.; Labriola, C.A.; Landolfo, L.; Delfino, J.M.; Parodi, A.J.; Caramelo, J.J. "The structure of calreticulin C-terminal domain is modulated by physiological variations of calcium concentration" (2010) Journal of Biological Chemistry. 285(7):4544-4553
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Abstract:

Calreticulin is an abundant endoplasmic reticulum resident protein that fulfills at least two basic functions. Firstly, due to its ability to bind monoglucosylated high mannose oligosaccharides, calreticulin is a central component of the folding quality control system of glycoproteins.Onthe other hand, thanks to its capacity to bind high amounts of calcium, calreticulin is one of the main calcium buffers in the endoplasmic reticulum. This last activity resides on a highly negatively charged domain located at the C terminus. Interestingly, this domain has been proposed to regulate the intracellular localization of calreticulin. Structural information for this domain is currently scarce. Here we address this issue by employing a combination of biophysical techniques and molecular dynamics simulation. We found that calreticulin C-terminal domain at low calcium concentration displays a disordered structure, whereas calcium addition induces a more rigid and compact conformation. Remarkably, this change develops when calcium concentration varies within a range similar to that taking place in the endoplasmic reticulum upon physiological fluctuations. In addition, a much higher calcium concentration is necessary to attain similar responses in a peptide displaying a randomized sequence of calreticulin C-terminal domain, illustrating the sequence specificity of this effect. Molecular dynamics simulation reveals that this ordering effect is a consequence of the ability of calcium to bring into close proximity residues that lie apart in the primary structure. These results place calreticulin in a new setting in which the protein behaves not only as a calcium-binding protein but as a finely tuned calcium sensor. © 2010 by The American Society for Biochemistry and Molecular Biology, Inc.

Registro:

Documento: Artículo
Título:The structure of calreticulin C-terminal domain is modulated by physiological variations of calcium concentration
Autor:Giraldo, A.M.V.; Medus, M.L.; Lebrero, M.G.; Pagano, R.S.; Labriola, C.A.; Landolfo, L.; Delfino, J.M.; Parodi, A.J.; Caramelo, J.J.
Filiación:Laboratory of Structural Cell Biology, Fundación Instituto Leloir, Instituto de Investigaciones Bioquímicas de Buenos Aires, C1405BWE Buenos Aires, Argentina
Laboratory of Glycobiology, Fundación Instituto Leloir, Instituto de Investigaciones Bioquímicas de Buenos Aires, Avenida Patricias Argentinas 435, C1405BWE Buenos Aires, Argentina
Department of Biological Chemistry, School of Pharmacy and Biochemistry, University of Buenos Aires, C1113AADD Buenos Aires, Argentina
Department of Biological Chemistry, School of Sciences, University of Buenos Aires, 1428 Buenos Aires, Argentina
Palabras clave:Basic functions; Biophysical techniques; C terminus; C-terminal domains; Calcium addition; Calcium binding proteins; Calcium concentration; Calcium sensors; Calreticulin; Central component; Close proximity; Disordered structures; Endoplasmic reticulum; Intracellular localization; Molecular dynamics simulations; Ordering effects; Primary structures; Randomized sequence; Sequence specificity; Structural information; Calcium; Concentration (process); Customer satisfaction; Molecular dynamics; Molecular mechanics; Proteins; Rigid structures; Total quality management; Calcium alloys; calcium; calreticulin; article; biophysics; calcium cell level; calcium transport; carboxy terminal sequence; circular dichroism; conformational transition; controlled study; endoplasmic reticulum; molecular dynamics; molecular model; priority journal; protein conformation; protein domain; protein secondary structure; protein structure; simulation; Animals; Calcium; Calreticulin; Chromatography, Gel; Circular Dichroism; Fourier Analysis; Protein Structure, Secondary; Protein Structure, Tertiary; Rabbits
Año:2010
Volumen:285
Número:7
Página de inicio:4544
Página de fin:4553
DOI: http://dx.doi.org/10.1074/jbc.M109.034512
Título revista:Journal of Biological Chemistry
Título revista abreviado:J. Biol. Chem.
ISSN:00219258
CODEN:JBCHA
CAS:calcium, 14092-94-5, 7440-70-2; Calcium, 7440-70-2; Calreticulin
Registro:https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_00219258_v285_n7_p4544_Giraldo

Referencias:

  • Mery, L., Mesaeli, N., Michalak, M., Opas, M., Lew, D.P., Krause, K.H., (1996) J. Biol. Chem., 271, pp. 9332-9339
  • Labriola, C., Cazzulo, J.J., Parodi, A.J., (1999) Mol. Biol. Cell, 10, pp. 1381-1394
  • Michalak, M., Corbett, E.F., Mesaeli, N., Nakamura, K., Opas, M., (1999) Biochem. J., 344, pp. 281-292
  • Burns, K., Duggan, B., Atkinson, E.A., Famulski, K.S., Nemer, M., Bleackley, R.C., Michalak, M., (1994) Nature, 367, pp. 476-480
  • Dedhar, S., Rennie, P.S., Shago, M., Hagesteijn, C.Y., Yang, H., Filmus, J., Hawley, R.G., Giguére, V., (1994) Nature, 367, pp. 480-483
  • Coppolino, M.G., Woodside, M.J., Demaurex, N., Grinstein, S., St-Arnaud, R., Dedhar, S., (1997) Nature, 386, pp. 843-847
  • Holaska, J.M., Black, B.E., Rastinejad, F., Paschal, B.M., (2002) Mol. Cell. Biol., 22, pp. 6286-6297
  • Nauseef, W.M., McCormick, S.J., Clark, R.A., (1995) J. Biol. Chem., 270, pp. 4741-4747
  • Spiro, R.G., Zhu, Q., Bhoyroo, V., Söling, H.D., (1996) J. Biol. Chem., 271, pp. 11588-11594
  • Caramelo, J.J., Parodi, A.J., (2008) J. Biol. Chem., 283, pp. 10221-10225
  • Vassilakos, A., Michalak, M., Lehrman, M.A., Williams, D.B., (1998) Biochemistry, 37, pp. 3480-3490
  • Van Der Wal, F.J., Oliver, J.D., High, S., (1998) Eur. J. Biochem., 256, pp. 51-59
  • Molinari, M., Helenius, A., (1999) Nature, 402, pp. 90-93
  • Jannatipour, M., Rokeach, L.A., (1995) J. Biol. Chem., 270, pp. 4845-4853
  • Parlati, F., Dignard, D., Bergeron, J.J., Thomas, D.Y., (1995) EMBO J., 14, pp. 3064-3072
  • Molinari, M., Eriksson, K.K., Calanca, V., Galli, C., Cresswell, P., Michalak, M., Helenius, A., (2004) Mol. Cell, 13, pp. 125-135
  • Nakamura, K., Zuppini, A., Arnaudeau, S., Lynch, J., Ahsan, I., Krause, R., Papp, S., Michalak, M., (2001) J. Cell Biol., 154, pp. 961-972
  • Guo, L., Nakamura, K., Lynch, J., Opas, M., Olson, E.N., Agellon, L.B., Michalak, M., (2002) J. Biol. Chem., 277, pp. 50776-50779
  • Smith, M.J., Koch, G.L., (1989) EMBO J., 8, pp. 3581-3586
  • Schrag, J.D., Bergeron, J.J., Li, Y., Borisova, S., Hahn, M., Thomas, D.Y., Cygler, M., (2001) Mol. Cell, 8, pp. 633-644
  • Ellgaard, L., Riek, R., Herrmann, T., Güntert, P., Braun, D., Helenius, A., Wüthrich, K., (2001) Proc. Natl. Acad. Sci. U.S.A., 98, pp. 3133-3138
  • Frickel, E.M., Riek, R., Jelesarov, I., Helenius, A., Wuthrich, K., Ellgaard, L., (2002) Proc. Natl. Acad. Sci. U.S.A., 99, pp. 1954-1959
  • Conte, I.L., Keith, N., Gutiérrez-Gonzalez, C., Parodi, A.J., Caramelo, J.J., (2007) Biochemistry, 46, pp. 4671-4680
  • Leach, M.R., Cohen-Doyle, M.F., Thomas, D.Y., Williams, D.B., (2002) J. Biol. Chem., 277, pp. 29686-29697
  • Baksh, S., Michalak, M., (1991) J. Biol. Chem., 266, pp. 21458-21465
  • Sönnichsen, B., Füllekrug, J., Nguyen Van, P., Diekmann, W., Robinson, D.G., Mieskes, G., (1994) J. Cell Sci., 107, pp. 2705-2717
  • Afshar, N., Black, B.E., Paschal, B.M., (2005) Mol. Cell. Biol., 25, pp. 8844-8853
  • Nørgaard Toft, K., Larsen, N., Steen Jørgensen, F., Højrup, P., Houen, G., Vestergaard, B., (2008) Biochim. Biophys. Acta, 1784, pp. 1265-1270
  • Henry, E.R., Hofrichter, J., (1992) Methods Enzymol., 210, pp. 129-192
  • Mukhopadhyay, K., Basak, S., (1998) Biophys. Chem., 74, pp. 175-186
  • Van Der Spoel, D., Lindahl, E., Hess, B., Groenhof, G., Mark, A.E., Berendsen, H.J.C., (2005) J. Comp. Chem., 26, pp. 1701-1718
  • Essman, U., Perela, L., Berkowitz, M.L., Darden, T., Lee, H., Pedersen, L.G., (1995) J. Chem. Phys., 103, pp. 8577-8592
  • Gunsteren, W.F., Berendsen, H.J., (1990) Angew. Chem. Int. Ed. Engl., 29, pp. 992-1023
  • Berendsen, H.J., Postma, J.V., (1984) J. Chem. Phys., 81, pp. 3684-3690
  • Nelson, J.W., Kallenbach, N.R., (1986) Proteins, 1, pp. 211-217
  • Storrs, R.W., Truckses, D., Wemmer, D.E., (1992) Biopolymers, 32, pp. 1695-1702
  • Li, Z., Stafford, W.F., Bouvier, M., (2001) Biochemistry, 40, pp. 11193-11201
  • Tan, Y., Chen, M., Li, Z., Mabuchi, K., Bouvier, M., (2006) Biochim. Biophys. Acta, 1760, pp. 745-753
  • Corbett, E.F., Michalak, K.M., Oikawa, K., Johnson, S., Campbell, I.D., Eggleton, P., Kay, C., Michalak, M., (2000) J. Biol. Chem., 275, pp. 27177-27185
  • Rizvi, S.M., Mancino, L., Thammavongsa, V., Cantley, R.L., Raghavan, M., (2004) Mol. Cell, 15, pp. 913-923
  • Miyawaki, A., Llopis, J., Heim, R., McCaffery, J.M., Adams, J.A., Ikura, M., Tsien, R.Y., (1997) Nature, 388, pp. 882-887
  • Yu, R., Hinkle, P.M., (2000) J. Biol. Chem., 275, pp. 23648-23653
  • Muñoz, V., Serrano, L., (1994) Nat. Struct. Biol., 1, pp. 399-409
  • Bouvier, M., Stafford, W.F., (2000) Biochemistry, 39, pp. 14950-14959
  • Tufi, R., Panaretakis, T., Bianchi, K., Criollo, A., Fazi, B., Di Sano, F., Tesniere, A., Kroemer, G., (2008) Cell Death Differ., 15, pp. 274-282

Citas:

---------- APA ----------
Giraldo, A.M.V., Medus, M.L., Lebrero, M.G., Pagano, R.S., Labriola, C.A., Landolfo, L., Delfino, J.M.,..., Caramelo, J.J. (2010) . The structure of calreticulin C-terminal domain is modulated by physiological variations of calcium concentration. Journal of Biological Chemistry, 285(7), 4544-4553.
http://dx.doi.org/10.1074/jbc.M109.034512
---------- CHICAGO ----------
Giraldo, A.M.V., Medus, M.L., Lebrero, M.G., Pagano, R.S., Labriola, C.A., Landolfo, L., et al. "The structure of calreticulin C-terminal domain is modulated by physiological variations of calcium concentration" . Journal of Biological Chemistry 285, no. 7 (2010) : 4544-4553.
http://dx.doi.org/10.1074/jbc.M109.034512
---------- MLA ----------
Giraldo, A.M.V., Medus, M.L., Lebrero, M.G., Pagano, R.S., Labriola, C.A., Landolfo, L., et al. "The structure of calreticulin C-terminal domain is modulated by physiological variations of calcium concentration" . Journal of Biological Chemistry, vol. 285, no. 7, 2010, pp. 4544-4553.
http://dx.doi.org/10.1074/jbc.M109.034512
---------- VANCOUVER ----------
Giraldo, A.M.V., Medus, M.L., Lebrero, M.G., Pagano, R.S., Labriola, C.A., Landolfo, L., et al. The structure of calreticulin C-terminal domain is modulated by physiological variations of calcium concentration. J. Biol. Chem. 2010;285(7):4544-4553.
http://dx.doi.org/10.1074/jbc.M109.034512