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Retracted. Lectin-deficient calreticulin retains full functionality as a chaperone for class I histocompatibility molecules

Retracted. Lectin-deficient calreticulin retains full functionality as a chaperone for class I histocompatibility molecules
Retracted. Lectin-deficient calreticulin retains full functionality as a chaperone for class I histocompatibility molecules
The authors of “Lectin-deficient Calreticulin Retains Full Functionality as a Chaperone for Class I Histocompatibility Molecules” (Mol. Biol. Cell [2008] 19, 2413–2423; originally published in MBoC In Press as 10.1091/mbc.E07-10-1055) wish to retract their paper. They have provided the following statement:
Our paper reported that two lectin-deficient mutants of calreticulin retained full ability to support the biogenesis of class I histocompatibility molecules and also bound to the same spectrum of newly synthesized glycoproteins as the wild-type chaperone. During recent efforts to extend this work, we were unable to replicate the results. An investigation detected evidence of contaminating wild-type calreticulin in the original mutant cell lines, contamination that occurred by unknown means in the senior author's laboratory. Consequently, we wish to retract the paper. We continue to work on the nature of the interactions of calreticulin with client glycoproteins and will be publishing thoroughly validated results on this issue in the near future. We offer our most sincere apologies to the scientific community for any difficulties that may have been experienced. All of the authors have agreed to this retraction.

Original abstract:
Calreticulin is a molecular chaperone of the endoplasmic reticulum that uses both a lectin site specific for Glc1Man5-9GlcNAc2 oligosaccharides and a polypeptide binding site to interact with nascent glycoproteins. The latter mode of substrate recognition is controversial. To examine the relevance of polypeptide binding to protein folding in living cells, we prepared lectin-deficient mutants of calreticulin and examined their abilities to support the assembly and quality control of mouse class I histocompatibility molecules. In cells lacking calreticulin, class I molecules exhibit inefficient loading of peptide ligands, reduced cell surface expression and aberrantly rapid export from the endoplasmic reticulum. Remarkably, expression of calreticulin mutants that are completely devoid of lectin function fully complemented all of the class I biosynthetic defects. We conclude that calreticulin can use nonlectin-based modes of substrate interaction to effect its chaperone and quality control functions on class I molecules in living cells. Furthermore, pulse-chase coimmunoisolation experiments revealed that lectin-deficient calreticulin bound to a similar spectrum of client proteins as wild-type calreticulin and dissociated with similar kinetics, suggesting that lectin-independent interactions are commonplace in cells and that they seem to be regulated during client protein maturation.
1059-1524
2413-2423
Ireland, Breanna S.
453f7f1e-362e-4e89-bbd6-647509a7910d
Brockmeier, Ulf
9b016802-917e-45b0-a66e-e522973e4537
Howe, Christopher M.
b57009ee-8bb9-4f95-9f17-cbc1a59a88a9
Elliott, Tim
16670fa8-c2f9-477a-91df-7c9e5b453e0e
Williams, David B.
df9861fe-10e3-4cff-af42-6c9ee36a8a2f
Ireland, Breanna S.
453f7f1e-362e-4e89-bbd6-647509a7910d
Brockmeier, Ulf
9b016802-917e-45b0-a66e-e522973e4537
Howe, Christopher M.
b57009ee-8bb9-4f95-9f17-cbc1a59a88a9
Elliott, Tim
16670fa8-c2f9-477a-91df-7c9e5b453e0e
Williams, David B.
df9861fe-10e3-4cff-af42-6c9ee36a8a2f

Ireland, Breanna S., Brockmeier, Ulf, Howe, Christopher M., Elliott, Tim and Williams, David B. (2008) Retracted. Lectin-deficient calreticulin retains full functionality as a chaperone for class I histocompatibility molecules. Molecular Biology of the Cell, 19 (6), 2413-2423. (doi:10.1091/mbc.E07-10-1055). (PMID:18337472)

Record type: Article

Abstract

The authors of “Lectin-deficient Calreticulin Retains Full Functionality as a Chaperone for Class I Histocompatibility Molecules” (Mol. Biol. Cell [2008] 19, 2413–2423; originally published in MBoC In Press as 10.1091/mbc.E07-10-1055) wish to retract their paper. They have provided the following statement:
Our paper reported that two lectin-deficient mutants of calreticulin retained full ability to support the biogenesis of class I histocompatibility molecules and also bound to the same spectrum of newly synthesized glycoproteins as the wild-type chaperone. During recent efforts to extend this work, we were unable to replicate the results. An investigation detected evidence of contaminating wild-type calreticulin in the original mutant cell lines, contamination that occurred by unknown means in the senior author's laboratory. Consequently, we wish to retract the paper. We continue to work on the nature of the interactions of calreticulin with client glycoproteins and will be publishing thoroughly validated results on this issue in the near future. We offer our most sincere apologies to the scientific community for any difficulties that may have been experienced. All of the authors have agreed to this retraction.

Original abstract:
Calreticulin is a molecular chaperone of the endoplasmic reticulum that uses both a lectin site specific for Glc1Man5-9GlcNAc2 oligosaccharides and a polypeptide binding site to interact with nascent glycoproteins. The latter mode of substrate recognition is controversial. To examine the relevance of polypeptide binding to protein folding in living cells, we prepared lectin-deficient mutants of calreticulin and examined their abilities to support the assembly and quality control of mouse class I histocompatibility molecules. In cells lacking calreticulin, class I molecules exhibit inefficient loading of peptide ligands, reduced cell surface expression and aberrantly rapid export from the endoplasmic reticulum. Remarkably, expression of calreticulin mutants that are completely devoid of lectin function fully complemented all of the class I biosynthetic defects. We conclude that calreticulin can use nonlectin-based modes of substrate interaction to effect its chaperone and quality control functions on class I molecules in living cells. Furthermore, pulse-chase coimmunoisolation experiments revealed that lectin-deficient calreticulin bound to a similar spectrum of client proteins as wild-type calreticulin and dissociated with similar kinetics, suggesting that lectin-independent interactions are commonplace in cells and that they seem to be regulated during client protein maturation.

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e-pub ahead of print date: 12 March 2008
Published date: 1 June 2008

Identifiers

Local EPrints ID: 80126
URI: http://eprints.soton.ac.uk/id/eprint/80126
ISSN: 1059-1524
PURE UUID: ec737f40-71a2-417a-884e-0dd875800539
ORCID for Tim Elliott: ORCID iD orcid.org/0000-0003-1097-0222

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Date deposited: 24 Mar 2010
Last modified: 14 Mar 2024 02:45

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Contributors

Author: Breanna S. Ireland
Author: Ulf Brockmeier
Author: Christopher M. Howe
Author: Tim Elliott ORCID iD
Author: David B. Williams

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