In vitro reconstitution of calreticulin-substrate interactions

QUICK SEARCH:

[advanced]

	Author:		Keyword(s):

Home Help Feedback Subscriptions Archive Search Table of Contents

This Article

	Summary
	Full Text (PDF)
	Alert me when this article is cited
	Alert me if a correction is posted

Services

	Email this article to a friend
	Similar articles in this journal
	Similar articles in PubMed
	Alert me to new issues of the journal
	Download to citation manager


Citing Articles

	Citing Articles via HighWire
	Citing Articles via Google Scholar

Google Scholar

	Articles by Peterson, J. R.
	Articles by Helenius, A.
	Search for Related Content

PubMed

	PubMed Citation
	Articles by Peterson, J. R.
	Articles by Helenius, A.

Braakman, I., Hoover-Litty, H., Wagner, K. R. and Helenius, A (1991). Folding of influenza hemagglutinin in the endoplasmic reticulum. J. Cell Biol 114, 401-411.[Abstract/Free Full Text]

Cannon, K. and Helenius, A (1999). Trimming and readdition of glucose to N-linked oligosaccharides determines calnexin association of a substrate glycoprotein in living cells. J. Biol. Chem 274, 7537-7544.[Abstract/Free Full Text]

Chen, W., Helenius, J., Braakman, I. and Helenius, A (1995). Cotranslational folding and calnexin binding during glycoprotein synthesis. Proc. Nat. Acad. Sci. USA 92, 6229-6233.[Abstract/Free Full Text]

David, V., Hochstenbach, F., Rajagopalan, S. and Brenner, M. B (1993). Interaction with newly synthesized and retained proteins in the endoplasmic reticulum suggests a chaperone function for human integral membrane protein IP90 (calnexin). J. Biol. Chem 268, 9585-9592.[Abstract/Free Full Text]

De Silva, A., Balch, W. E. and Helenius, A (1990). Quality control in the endoplasmic reticulum: folding and misfolding of vesicular stomatitis virus G protein in cells and in vitro. J. Cell Biol 111, 857-866.[Abstract/Free Full Text]

Doms, R. W., Helenius, A. and White, J. M (1985). Membrane fusion activity of the influenza virus hemagglutinin: the low pH-induced conformational change. J. Biol. Chem 260, 2973-2981.[Abstract/Free Full Text]

Doxsey, S. J., Sambrook, J., Helenius, A. and White, J (1985). An efficient method for introducing macromoleculues into living cells. J. Cell Biol 101, 19-27.[Abstract/Free Full Text]

Elliott, J. G., Oliver, J. D. and High, S (1997). The thiol-dependent reductase ERp57 interacts specifically with N-glycosylated integral membrane proteins. J. Biol. Chem 272, 13849-13855.[Abstract/Free Full Text]

Gallione, C. J. and Rose, J. K (1985). A single amino acid substitution in a hydrophobic domain causes temperature-sensitive cell-surface transport of a mutant viral glycoprotein. J. Cell Biol 108, 811-819.[Abstract/Free Full Text]

Guan, K. and Dixon, J. E (1991). Eukaryotic proteins expressed in Escherichia coli : An improved thrombin cleavage and purification procedure of fusion proteins with glutathione S-transferase. Anal. Biochem 192, 262-267.[Medline]

Halaban, R., Cheng, E., Zhang, Y. H., Moellmann, G., Hanlon, D., Michalak, M., Setaluri, V. and Hebert, D. N (1997). Aberrant retention of tyrosinase in the endoplasmic reticulum mediates accelerated degradation of the enzyme and contributes to the dedifferentiated phenotype of amelanotic melanoma cells. Proc. Nat. Acad. Sci. USA 94, 6210-6215.[Abstract/Free Full Text]

Hammond, C. and Helenius, A (1994). Folding of VSV G protein: sequential interaction with BiP and calnexin. Science 266, 456-458.[Abstract/Free Full Text]

Hammond, C. and Helenius, A (1994). Quality control in the secretory pathway: retention of a misfolded viral membrane glycoprotein involves cycling between the ER, intermediate compartment and Golgi apparatus. J. Cell Biol 126, 41-52.[Abstract/Free Full Text]

Hammond, C., Braakman, I. and Helenius, A (1994). Role of N-linked oligosaccharides, glucose trimming and calnexin in glycoprotein folding and quality control. Proc. Nat. Acad. Sci. USA 91, 913-917.[Abstract/Free Full Text]

Hebert, D. N., Foellmer, B. and Helenius, A (1995). Glucose trimming and reglucosylation determine glycoprotein association with calnexin in the endoplasmic reticulum. Cell 81, 425-433.[Medline]

Hebert, D. N., Foellmer, B. and Helenius, A (1997). The number and location of glycans on influenza hemagglutinin determine folding and association with calnexin and calreticulin. J. Cell Biol 139, 613-623.[Abstract/Free Full Text]

Hebert, D. N., Foellmer, B. and Helenius, A (1996). Calnexin and calreticulin promote folding, delay oligomerization and suppress degradation of influenza hemagglutinin in microsomes. EMBO J 15, 2961-2968.[Medline]

Helenius, A (1994). How N-linked oligosaccharides affect glycoprotein folding in the endoplasmic reticulum. Mol. Biol. Cell 5, 253-265.[Medline]

Ikawa, M., Wada, I., Kominami, K., Watanabe, D., Toshimori, K., Nishimune, Y. and Okabe, M (1997). The putative chaperone calmegin is required for sperm fertility. Nature 387, 607-611.[Medline]

Jackson, M. R., Cohen-Doyle, M. R., Peterson, P. A. and Williams, D. B (1994). Regulation of MHC Class I transport by the molecular chaperone, calnexin (p88, IP90). Science 263, 384-387.[Abstract/Free Full Text]

Kearse, K. P., Williams, D. B. and Singer, A (1994). Persistence of glucose residues on core oligosaccharides prevents association of TCRand TCR proteins with calnexin and results specifically in accelerated degradation of nascent TCRa proteins within the endoplasmic reticulum. EMBO J 13, 3678-3686.[Medline]

Lin, P., Le-Niculescu, H., Hofmeister, R., McCaffery, J. M., Jin, M., Hennemann, H., McQuistan, T., Vries, L. D. and Farquhar, M. G (1998). The mammalian calcium-binding protein, nucleobindin (CALNUC), is a golgi resident protein. J. Cell. Biol 141, 1515-1527.[Abstract/Free Full Text]

Lindquist, J. A., Jensen, O. N., Mann, M. and Haemmerling, G. J (1998). ER-60, a chaperone with thiol-dependent reductase activity involved in MHC class I assembly. EMBO J 17, 2186-2195.[Medline]

Michalak, M., Milner, R. E., Burns, K. and Opas, M (1992). Calreticulin. [Review]. Biochem J 285, 681-692.

Nauseef, W. M., McCormick, S. J. and Clark, R. A (1995). Calreticulin functions as a molecular chaperone in the biosynthesis of myeloperoxidase. J. Biol. Chem 270, 4741-4747.[Abstract/Free Full Text]

Ohsako, S., Hayashi, Y. and Bunick, D (1994). Molecular cloning and sequencing of calnexin-t. J. Biol. Chem 269, 14140-14148.[Abstract/Free Full Text]

Oliver, J. D., Hresko, R. C., Mueckler, M. and High, S (1996). The glut 1 glucose transporter interacts with calnexin and calreticulin. J. Biol. Chem 271, 13691-13696.[Abstract/Free Full Text]

Oliver, J. D., Vanderwal, F. J., Bulleid, N. J. and High, S (1997). Interaction of the thiol-dependent reductase ERp57 with nascent glycoproteins. Science 275, 86-88.[Abstract/Free Full Text]

Ortmann, B., Copeman, J., Lehner, P. J., Sadasivan, B., Herberg, J. A., Grandea, A. G., Riddell, S. R., Tampe, R., Spies, T., Trowsdale, J. et al (1997). A critical role for tapasin in the assembly and function of multimeric MHC class I-TAP complexes. Science 277, 1306-1309.[Abstract/Free Full Text]

Otteken, A. and Moss, B (1996). Calreticulin interacts with newly synthesized human immunodeficiency virus type 1 envelope glycoprotein, suggesting a chaperone function similar to that of calnexin. J. Biol. Chem 271, 97-103.[Abstract/Free Full Text]

Parodi, A. J., Mendelzon, G. Z., Lederkremer, G. Z. and Martin-Barrientos, J (1984). Evidence that transient glucosylation of protein-linked Man9GlcNAc2,Man8GlcNAc2,and Man7GlcNAc2 occurs in rat liver and Phaseolus vulgaris cells. J. Biol. Chem 259, 6351-6357.[Abstract/Free Full Text]

Peterson, J. R., Ora, A., Van, P. N. and Helenius, A (1995). Transient, lectin-like association of calreticulin with folding intermediates of cellular and viral glycoproteins. Mol. Biol. Cell 6, 1173-1184.[Abstract]

Pipe, S. W., Morris, J. A., Shah, J. and Kaufman, R. J (1998). Differential interaction of coagulation factor VII and factor V with protein chaperones calnexin and calreticulin. J. Biol. Chem 273, 8537-8544.[Abstract/Free Full Text]

Sadasivan, B., Lehner, P. J., Ortmann, B., Spies, T. and Cresswell, P (1996). Roles for calreticulin and a novel glycoprotein, tapasin, in the interaction of MHC class I molecules with TAP. Immunity 5, 103-114.[Medline]

S\232nnichsen, B., Fullekrug, J., Nguyen, V. P., Diekmann, W., Robinson, D. G. and Mieskes, G (1994). Retention and retrieval: both mechanisms cooperate to maintain calreticulin in the endoplasmic reticulum. J. Cell Sci 107, 2705-2717.[Abstract]

Sousa, M. C., Ferrero-Garcia, M. A. and Parodi, A. J (1992). Recognition of the oligosaccharide and protein moieties of glycoproteins by the UDP-Glc:glycoprotein glucosyltransferase. Biochemistry 31, 97-105.[Medline]

Sousa, M. and Parodi, A. J (1995). The molecular basis for the recognition of misfolded glycoproteins by the UDP-Glc:glycoprotein glucosyltransferase. EMBO J 14, 4196-4203.[Medline]

Spiro, R. G., Zhu, Q., Bhoyroo, V. and S\232ling, H.-D (1996). Definition of the lectin-like properties of the molecular chaperone, calreticulin, and demonstration of its copurification with endomannosidase from rat liver golgi. J. Biol. Chem 271, 11588-11594.[Abstract/Free Full Text]

Suh, K., Bergmann, J. E. and Gabel, C. A (1989). Selective retention of monoglucosylated high mannose oligosaccharides by a class of mutant vesicular stomatitis virus G proteins. J. Cell Biol 108, 811-819.

Tector, M. and Salter, R. D (1995). Calnexin influences folding of human class I histocompatibility proteins but not their assembly with2-microglobulin. J. Biol. Chem 270, 19638-19642.[Abstract/Free Full Text]

Trombetta, E. S., Simons, J. F. and Helenius, A (1996). Endoplasmic reticulum glucosidase II is composed of a catalytic subunit, conserved fromyeast to mammals, and a tightly bound noncatalytic HDEL-containing subunit. J. Biol. Chem 271, 27509-27516.[Abstract/Free Full Text]

Trombetta, E. S., Ganan, S. and Parodi, A. J (1991). The UDP-Glc:glycoprotein glucosyltransferase is a soluble protein of the endoplasmic reticulum. Glycobiology 1, 155-161.[Abstract/Free Full Text]

van Leeuwen, J. E. M. and Kearse, K. P (1996). The related molecular chaperones calnexin and calreticulin differentially associate with nascent T cell antigen receptor proteins within the endoplasmic reticulum. J. Biol. Chem 271, 25345-25349.[Abstract/Free Full Text]

Vassilakos, A., Cohen, D. M., Peterson, P. A., Jackson, M. R. and Williams, D. B (1996). The molecular chaperone calnexin facilitates folding and assembly of class I histocompatibility molecules. EMBOJ 15, 1495-1506.[Medline]

Vassilakos, A., Michalak, M., Lehrman, M. A. and Williams, D. B (1998). Oligosaccharide binding characteristics of the molecular chaperones calnexin and calreticulin. Biochemistry 37, 3480-3490.[Medline]

Wada, I., Rindress, D., Cameron, P. H., Ou, W., Doherty, J. J., Louvard, D., Bell, A. W., Dignard, D., Thomas, D. Y. and Bergeron, J. J. M (1991). SSRand associated calnexin are major calcium binding proteins of the endoplasmic reticulum membrane. J. Biol. Chem 266, 19599-19610.[Abstract/Free Full Text]

Wada, I., Kai, M., Imai, S., Sakane, F. and Kanoh, H (1997). Promotion of transferrin folding by cyclic interactions with calnexin and calreticulin. EMBO J 16, 5420-5432.[Medline]

Ware, F. E., Vassilakos, A., Peterson, P. A., Jackson, M. R., Lehrman, M. A. and Williams, D. B (1995). The molecular chaperone calnexin binds Glc1Man9GlcNAc2 oligosaccharide as an initial step in recognizing unfolded glycoproteins. J. Biol. Chem 270, 4697-4707.[Abstract/Free Full Text]

Williams, D. B (1995). Calnexin: a molecular chaperone with a taste for carbohydrate. Biochem. Cell Biol 73, 123-132.[Medline]

Zapun, A., Petrescu, S. M., Rudd, P. M., Dwek, R. A., Thomas, D. Y. and Bergeron, J (1997). Conformation-independent binding of monoglucosylated ribonuclease Bto calnexin. Cell 88, 29-38.[Medline]

Zapun, A., Darby, N. J., Tessier, D. C., Michalak, M., Bergeron, J. J. M. and Thomas, D. Y (1998). Enhanced catalysis of ribonuclease B folding by the interaction of calnexin or calreticulin with ERp57. J. Biol. Chem 273, 6009-6012.[Abstract/Free Full Text]

This article has been cited by other articles:

E. L. Snapp, A. Sharma, J. Lippincott-Schwartz, and R. S. Hegde
Monitoring chaperone engagement of substrates in the endoplasmic reticulum of live cells
PNAS, April 25, 2006; 103(17): 6536 - 6541.
[Abstract] [Full Text] [PDF]

P. A. Wearsch, C. A. Jakob, A. Vallin, R. A. Dwek, P. M. Rudd, and P. Cresswell
Major Histocompatibility Complex Class I Molecules Expressed with Monoglucosylated N-Linked Glycans Bind Calreticulin Independently of Their Assembly Status
J. Biol. Chem., June 11, 2004; 279(24): 25112 - 25121.
[Abstract] [Full Text] [PDF]

L. Silvennoinen, J. Myllyharju, M. Ruoppolo, S. Orru, M. Caterino, K. I. Kivirikko, and P. Koivunen
Identification and Characterization of Structural Domains of Human ERp57: ASSOCIATION WITH CALRETICULIN REQUIRES SEVERAL DOMAINS
J. Biol. Chem., April 2, 2004; 279(14): 13607 - 13615.
[Abstract] [Full Text] [PDF]

E. S. Trombetta
The contribution of N-glycans and their processing in the endoplasmic reticulum to glycoprotein biosynthesis
Glycobiology, September 1, 2003; 13(9): 77R - 91R.
[Abstract] [Full Text] [PDF]

M. Kapoor, H. Srinivas, E. Kandiah, E. Gemma, L. Ellgaard, S. Oscarson, A. Helenius, and A. Surolia
Interactions of Substrate with Calreticulin, an Endoplasmic Reticulum Chaperone
J. Biol. Chem., February 14, 2003; 278(8): 6194 - 6200.
[Abstract] [Full Text] [PDF]

M. R. Leach, M. F. Cohen-Doyle, D. Y. Thomas, and D. B. Williams
Localization of the Lectin, ERp57 Binding, and Polypeptide Binding Sites of Calnexin and Calreticulin
J. Biol. Chem., August 9, 2002; 277(33): 29686 - 29697.
[Abstract] [Full Text] [PDF]

J. M. Holaska, B. E. Black, D. C. Love, J. A. Hanover, J. Leszyk, and B. M. Paschal
Calreticulin Is a Receptor for Nuclear Export
J. Cell Biol., January 8, 2001; 152(1): 127 - 140.
[Abstract] [Full Text] [PDF]

A Elagoz, M Callejo, J Armstrong, and L. Rokeach
Although calnexin is essential in S. pombe, its highly conserved central domain is dispensable for viability
J. Cell Sci., January 12, 1999; 112(23): 4449 - 4460.
[Abstract] [PDF]

L. Ellgaard, R. Riek, T. Herrmann, P. Guntert, D. Braun, A. Helenius, and K. Wuthrich
NMR structure of the calreticulin P-domain
PNAS, March 13, 2001; 98(6): 3133 - 3138.
[Abstract] [Full Text] [PDF]

This Article

Summary

Full Text (PDF)

Alert me when this article is cited

Alert me if a correction is posted

Services

Email this article to a friend

Similar articles in this journal

Similar articles in PubMed

Alert me to new issues of the journal

Download to citation manager

Citing Articles

Citing Articles via HighWire

Citing Articles via Google Scholar

Google Scholar

Articles by Peterson, J. R.

Articles by Helenius, A.

Search for Related Content

PubMed

PubMed Citation

Articles by Peterson, J. R.

Articles by Helenius, A.

				P. A. Wearsch, C. A. Jakob, A. Vallin, R. A. Dwek, P. M. Rudd, and P. Cresswell Major Histocompatibility Complex Class I Molecules Expressed with Monoglucosylated N-Linked Glycans Bind Calreticulin Independently of Their Assembly Status J. Biol. Chem., June 11, 2004; 279(24): 25112 - 25121. [Abstract] [Full Text] [PDF]

				L. Silvennoinen, J. Myllyharju, M. Ruoppolo, S. Orru, M. Caterino, K. I. Kivirikko, and P. Koivunen Identification and Characterization of Structural Domains of Human ERp57: ASSOCIATION WITH CALRETICULIN REQUIRES SEVERAL DOMAINS J. Biol. Chem., April 2, 2004; 279(14): 13607 - 13615. [Abstract] [Full Text] [PDF]

				E. S. Trombetta The contribution of N-glycans and their processing in the endoplasmic reticulum to glycoprotein biosynthesis Glycobiology, September 1, 2003; 13(9): 77R - 91R. [Abstract] [Full Text] [PDF]

				M. Kapoor, H. Srinivas, E. Kandiah, E. Gemma, L. Ellgaard, S. Oscarson, A. Helenius, and A. Surolia Interactions of Substrate with Calreticulin, an Endoplasmic Reticulum Chaperone J. Biol. Chem., February 14, 2003; 278(8): 6194 - 6200. [Abstract] [Full Text] [PDF]

				M. R. Leach, M. F. Cohen-Doyle, D. Y. Thomas, and D. B. Williams Localization of the Lectin, ERp57 Binding, and Polypeptide Binding Sites of Calnexin and Calreticulin J. Biol. Chem., August 9, 2002; 277(33): 29686 - 29697. [Abstract] [Full Text] [PDF]

				J. M. Holaska, B. E. Black, D. C. Love, J. A. Hanover, J. Leszyk, and B. M. Paschal Calreticulin Is a Receptor for Nuclear Export J. Cell Biol., January 8, 2001; 152(1): 127 - 140. [Abstract] [Full Text] [PDF]

				A Elagoz, M Callejo, J Armstrong, and L. Rokeach Although calnexin is essential in S. pombe, its highly conserved central domain is dispensable for viability J. Cell Sci., January 12, 1999; 112(23): 4449 - 4460. [Abstract] [PDF]

				L. Ellgaard, R. Riek, T. Herrmann, P. Guntert, D. Braun, A. Helenius, and K. Wuthrich NMR structure of the calreticulin P-domain PNAS, March 13, 2001; 98(6): 3133 - 3138. [Abstract] [Full Text] [PDF]