Calreticulin - Revision history

Carole Weaver: /* Knockout mouse lines */

2011-03-25T23:13:26Z

Knockout mouse lines

Kurt Drickamer: /* Knockout mouse lines */

2011-03-22T13:44:22Z

Knockout mouse lines

Kurt Drickamer: /* Biosynthesis of ligands */

2011-03-18T09:09:14Z

Biosynthesis of ligands

Kurt Drickamer: /* Acknowledgements */

2011-03-18T09:04:42Z

Acknowledgements

Kurt Drickamer: /* Biological roles of GBP-ligand interaction */

2011-03-17T17:48:40Z

Biological roles of GBP-ligand interaction

Kurt Drickamer at 17:42, 17 March 2011

2011-03-17T17:42:56Z

Kurt Drickamer: /* Structure */

2011-03-17T17:35:33Z

Structure

Kurt Drickamer: /* Biosynthesis of ligands */

2011-03-17T17:33:28Z

Biosynthesis of ligands

Kurt Drickamer: /* Biosynthesis of ligands */

2011-03-17T17:30:08Z

Biosynthesis of ligands

Kurt Drickamer: /* Cellular expression of GBP and ligands */

2011-03-17T17:29:30Z

Cellular expression of GBP and ligands

@@ Line 42: / Line 42: @@
 === Knockout mouse lines ===
-The CFG did not undertake creation of knockout mice for sialoadhesin because generation of such mice was already underway. The knockout is embryonic lethal, as a result of abnormalities in cardiac development, which may be related to the additional role of calreticulin in controlling Ca<sup>2+</sup> levels in cells.<ref name=”Mesaeili1999”>Mesaeli, N, Nakamura, K, Zvaritch, E, Dickie, P, Dziak, E, Krause, K-M, Opas, M, MacLennan,  DH and Michalak, M. (1999) Calreticulin Is essential for cardiac development. J. Cell Biol. 144, 857-868</ref>
+The CFG did not undertake creation of knockout mice for calreticulin because generation of such mice was already underway. The knockout is embryonic lethal, as a result of abnormalities in cardiac development, which may be related to the additional role of calreticulin in controlling Ca<sup>2+</sup> levels in cells.<ref name=”Mesaeili1999”>Mesaeli, N, Nakamura, K, Zvaritch, E, Dickie, P, Dziak, E, Krause, K-M, Opas, M, MacLennan,  DH and Michalak, M. (1999) Calreticulin Is essential for cardiac development. J. Cell Biol. 144, 857-868</ref>
 <br>

@@ Line 42: / Line 42: @@
 === Knockout mouse lines ===
-No data available.
+The CFG did not undertake creation of knockout mice for sialoadhesin because generation of such mice was already underway. The knockout is embryonic lethal, as a result of abnormalities in cardiac development, which may be related to the additional role of calreticulin in controlling Ca<sup>2+</sup> levels in cells.<ref name=”Mesaeili1999”>Mesaeli, N, Nakamura, K, Zvaritch, E, Dickie, P, Dziak, E, Krause, K-M, Opas, M, MacLennan,  DH and Michalak, M. (1999) Calreticulin Is essential for cardiac development. J. Cell Biol. 144, 857-868</ref>
 <br>

@@ Line 17: / Line 17: @@
 === Biosynthesis of ligands ===
-N-linked glycans generated by the core N-linked biosynthesis pathway ([http://www.functionalglycomics.org/glycomics/molecule/jsp/glycoEnzyme/geMolecule.jsp?slideNumber=default GT Database]), are trimmed by the action of ER glucosidases I and II to create the calreticulin ligand Glc<sub>1</sub>Man<sub>9</sub>GlcNAc<sub>2</sub>. The third and final glucose residue is removed by ER glucosidase II, thus destroying the ligand for calreticulin. If the glycoprotein remains incorrectly folded, glucosyltransferase adds back the glucose, regenerating the ligand for calreticulin. Cycles of deglucosylation and re-glucosylation continue until the protein is correctly folded.<ref name="Parodi2000">Parodi, A.J. (2000) Role of N-oligosaccharides endoplasmic reticulum processing reactions in glycoprotein folding and degradation. Biochem. J., 348, 1-13</ref>
+N-linked glycans generated by the core N-linked biosynthesis pathway ([http://www.functionalglycomics.org/glycomics/molecule/jsp/glycoEnzyme/geMolecule.jsp?slideNumber=default GT Database]), are trimmed by the action of ER glucosidases I and II to create the calreticulin ligand Glc<sub>1</sub>Man<sub>9</sub>GlcNAc<sub>2</sub>. The third and final glucose residue is removed by ER glucosidase II, thus destroying the ligand for calreticulin. If the glycoprotein remains incorrectly folded, UDP-glucose:glycoprotein glucosyltransferase adds back the glucose, regenerating the ligand for calreticulin. Cycles of deglucosylation and re-glucosylation continue until the protein is correctly folded.<ref name="Parodi2000">Parodi, A.J. (2000) Role of N-oligosaccharides endoplasmic reticulum processing reactions in glycoprotein folding and degradation. Biochem. J., 348, 1-13</ref>
 <br>

← Older revision		Revision as of 09:04, 18 March 2011
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	== Acknowledgements ==		== Acknowledgements ==
−	The CFG is grateful to the following PIs for their contributions to this wiki page: John Hanover	+	The CFG is grateful to the following PIs for their contributions to this wiki page: Kurt Drickamer, John Hanover

@@ Line 25: / Line 25: @@
 === Biological roles of GBP-ligand interaction ===
-Work in a number of laboratories suggests that calreticulin plays a role as a molecular chaperone acting in consort with components of the oligosaccharide processing machinery to ensure ER quality control by limiting the mobility of improperly folded proteins<ref name="Jorgensen 2003" /><ref name="Ellgaard 2003"/><ref name="Helenius 2004" /><ref name="Michalak 2009" /><ref>Gelebart, P., Opas, M. and Michalak, M. Calreticulin, a Ca2+-binding chaperone of the endoplasmic reticulum. Int J Biochem Cell Biol 37, 260-266 (2005)</ref><ref name="Wearsch 2008">Wearsch, P. A. and Cresswell, P. The quality control of MHC class I peptide loading. Curr Opin Cell Biol 20, 624-631 (2008)</ref>. Calreticulin has also been suggested to be a component of the peptide loading complex where it interacts with other ER resident proteins to produce class-I major histocompatibility complex (MHC-1) molecules<ref name="Wearsch 2008" /><ref>Raghavan, M., Del Cid, N., Rizvi, S. M. and Peters, L. R. MHC class I assembly: out and about. Trends Immunol 29, 436-443 (2008) </ref><ref>Howe, C., Garstka, M., Al-Balushi, M., Ghanem, E., Antoniou, A. N., Fritzsche, S., Jankevicius, G., Kontouli, N., Schneeweiss, C., Williams, A., Elliott, T. and Springer, S. Calreticulin-dependent recycling in the early secretory pathway mediates optimal peptide loading of MHC class I molecules. EMBO J 28, 3730-3744 (2009)</ref>.
+Calreticulin promotes correct folding of secretory glycoprotein. Both calreticulin and calnexin are resident in the ER. Calreticulin possesses a C-terminal ER-retention signal to localize it to the ER lumen, whereas calnexin is anchored to the ER membrane by a transmembrane domain.<ref name="Jorgensen 2003" /><ref name="Ellgaard 2003"/><ref name="Helenius 2004" /><ref name="Michalak 2009" /><ref>Gelebart, P., Opas, M. and Michalak, M. Calreticulin, a Ca<sup>2+</sup>-binding chaperone of the endoplasmic reticulum. Int J Biochem Cell Biol 37, 260-266 (2005)</ref><ref name="Wearsch 2008">Wearsch, P. A. and Cresswell, P. The quality control of MHC class I peptide loading. Curr Opin Cell Biol 20, 624-631 (2008)</ref>. Incorrectly folded glycoproteins are tagged with a single glucose residue that binds to calnexin or calreticulin. The process acts in a cycle, in which glucose is continually removed and then re-attached if the glycoprotein is incorrectly folded.<ref name=”Aebi1009”>Aebi, M., Bernasconi, R., Clerc, S., and Molinari, M. (2009). N-glycan structures: recognition and processing in the ER. Trends Biochem Sci 35, 74–82</ref><ref name=”Lederkremer2009”>Lederkremer, G.Z. (2009). Glycoprotein folding, quality control and ER-associated degradation. Cur. Opin. Struct. Biol. 19, 515–523</ref>
 <br>

← Older revision		Revision as of 17:42, 17 March 2011
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−	This family of GBPs is widespread in evolution ~~and plays a key role in ER quality control~~<ref name="Ellgaard 2003a">Ellgaard, L. and Frickel, E. M. Calnexin, calreticulin, and ERp57: teammates in glycoprotein folding. Cell Biochem Biophys 39, 223-247 (2003)</ref><ref name="Jorgensen 2003">Jorgensen, M. M., Bross, P. and Gregersen, N. Protein quality control in the endoplasmic reticulum. APMIS Suppl 86-91 (2003)</ref><ref name="Ellgaard 2003">Ellgaard, L. and Helenius, A. Quality control in the endoplasmic reticulum. Nat Rev Mol Cell Biol 4, 181-191 (2003)</ref><ref name="Helenius 2004">Helenius, A. and Aebi, M. Roles of N-linked glycans in the endoplasmic reticulum. Annu Rev Biochem 73, 1019-1049 (2004)</ref><ref>Molinari, M., Eriksson, K. K., Calanca, V., Galli, C., Cresswell, P., Michalak, M. and Helenius, A. Contrasting functions of calreticulin and calnexin in glycoprotein folding and ER quality control. Mol Cell 13, 125-135 (2004)</ref><ref>Deprez, P., Gautschi, M. and Helenius, A. More than one glycan is needed for ER glucosidase II to allow entry of glycoproteins into the calnexin/calreticulin cycle. Mol Cell 19, 183-195 (2005)</ref><ref>Wu, J. C., Liang, Z. Q. and Qin, Z. H. Quality control system of the endoplasmic reticulum and related diseases. Acta Biochim Biophys Sin (Shanghai) 38, 219-226 (2006) </ref><ref>Caramelo, J. J. and Parodi, A. J. Getting in and out from calnexin/calreticulin cycles. J Biol Chem 283, 10221-10225 (2008) </ref><ref name="Michalak 2009">Michalak, M., Groenendyk, J., Szabo, E., Gold, L. I. and Opas, M. Calreticulin, a multi-process calcium-buffering chaperone of the endoplasmic reticulum. Biochem J 417, 651-666 (2009)</ref>. Other ER chaperones ~~have been suggested to have “lectinic” properties including calnexin~~ <ref name="Ellgaard 2003a"/>, but calreticulin is the best studied of ~~this family~~.	+	Calreticulin and calnexin are components of the quality control system that promotes correct folding of proteins that enter the secretory pathway and targets misfolded proteins for degradation. This family of GBPs is widespread in evolution<ref name="Ellgaard 2003a">Ellgaard, L. and Frickel, E. M. Calnexin, calreticulin, and ERp57: teammates in glycoprotein folding. Cell Biochem Biophys 39, 223-247 (2003)</ref><ref name="Jorgensen 2003">Jorgensen, M. M., Bross, P. and Gregersen, N. Protein quality control in the endoplasmic reticulum. APMIS Suppl 86-91 (2003)</ref><ref name="Ellgaard 2003">Ellgaard, L. and Helenius, A. Quality control in the endoplasmic reticulum. Nat Rev Mol Cell Biol 4, 181-191 (2003)</ref><ref name="Helenius 2004">Helenius, A. and Aebi, M. Roles of N-linked glycans in the endoplasmic reticulum. Annu Rev Biochem 73, 1019-1049 (2004)</ref><ref>Molinari, M., Eriksson, K. K., Calanca, V., Galli, C., Cresswell, P., Michalak, M. and Helenius, A. Contrasting functions of calreticulin and calnexin in glycoprotein folding and ER quality control. Mol Cell 13, 125-135 (2004)</ref><ref>Deprez, P., Gautschi, M. and Helenius, A. More than one glycan is needed for ER glucosidase II to allow entry of glycoproteins into the calnexin/calreticulin cycle. Mol Cell 19, 183-195 (2005)</ref><ref>Wu, J. C., Liang, Z. Q. and Qin, Z. H. Quality control system of the endoplasmic reticulum and related diseases. Acta Biochim Biophys Sin (Shanghai) 38, 219-226 (2006) </ref><ref>Caramelo, J. J. and Parodi, A. J. Getting in and out from calnexin/calreticulin cycles. J Biol Chem 283, 10221-10225 (2008) </ref><ref name="Michalak 2009">Michalak, M., Groenendyk, J., Szabo, E., Gold, L. I. and Opas, M. Calreticulin, a multi-process calcium-buffering chaperone of the endoplasmic reticulum. Biochem J 417, 651-666 (2009)</ref>. Other ER chaperones are also glycan-binding proteins<ref name="Ellgaard 2003a"/>, but calreticulin and calnexin are the best studied examples of glycan-binding proteins involved in intracellular glycoprotein quality control.

	== CFG Participating Investigators contributing to the understanding of this paradigm ==		== CFG Participating Investigators contributing to the understanding of this paradigm ==

← Older revision		Revision as of 17:30, 17 March 2011
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	=== Biosynthesis of ligands ===		=== Biosynthesis of ligands ===
		+	N-linked glycans generated by the core N-linked biosynthesis pathway [LINK] are trimmed by the action of ER glucosidases I and II to create the calreticulin ligand Glc<sub>1</sub>Man<sub>9</sub>GlcNAc<sub>2</sub>. The third and final glucose residue is removed by ER glucosidase II, thus destroying the ligand for calreticulin. If the glycoprotein remains incorrectly folded, glucosyltransferase adds back the glucose, regenerating the ligand for calreticulin. Cycles of deglucosylation and re-glucosylation continue until the protein is correctly folded.<ref name="Parodi2000">Parodi, A.J. (2000) Role of N-oligosaccharides endoplasmic reticulum processing reactions in glycoprotein folding and degradation. Biochem. J., 348, 1-13</ref>
		+	<br>

−	~~<br>~~
	=== Structure ===		=== Structure ===

← Older revision		Revision as of 17:29, 17 March 2011
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	=== Cellular expression of GBP and ligands ===		=== Cellular expression of GBP and ligands ===
		+	Calnexin and calreticulin are ubiquitously expressed in the ER of all mammalian cell types.
		+	<br>

−	~~<br>~~
	=== Biosynthesis of ligands ===		=== Biosynthesis of ligands ===