A developmentally regulated chaperone complex for the endoplasmic reticulum of male haploid germ cells

Glycoprotein folding is mediated by lectin-like chaperones and protein disulfide isomerases (PDIs) in the endoplasmic reticulum. Calnexin and the PDI homologue ERp57 work together to help fold nascent polypeptides with glycans located toward the N-terminus of a protein, whereas PDI and BiP may engag...

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Bibliographic Details
Published in:Molecular biology of the cell 2007-08, Vol.18 (8), p.2795-2804
Main Authors: van Lith, Marcel, Karala, Anna-Riikka, Bown, Dave, Gatehouse, John A, Ruddock, Lloyd W, Saunders, Philippa T K, Benham, Adam M
Format: Article
Language:English
Subjects:
Animals
Antibody Specificity
Biophysical Phenomena
Biophysics
Calcium-Binding Proteins - metabolism
Endoplasmic Reticulum - metabolism
Gene Expression Regulation, Developmental
Haploidy
HeLa Cells
Humans
Male
Meiosis
Mice
Molecular Chaperones - metabolism
Polysaccharides - metabolism
Protein Binding
Protein Disulfide-Isomerases - genetics
Protein Disulfide-Isomerases - metabolism
Rats
Spermatozoa - cytology
Spermatozoa - enzymology
Spermatozoa - metabolism
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Summary:Glycoprotein folding is mediated by lectin-like chaperones and protein disulfide isomerases (PDIs) in the endoplasmic reticulum. Calnexin and the PDI homologue ERp57 work together to help fold nascent polypeptides with glycans located toward the N-terminus of a protein, whereas PDI and BiP may engage proteins that lack glycans or have sugars toward the C-terminus. In this study, we show that the PDI homologue PDILT is expressed exclusively in postmeiotic male germ cells, in contrast to the ubiquitous expression of many other PDI family members in the testis. PDILT is induced during puberty and represents the first example of a PDI family member under developmental control. We find that PDILT is not active as an oxido-reductase, but interacts with the model peptide Delta-somatostatin and nonnative bovine pancreatic trypsin inhibitor in vitro, indicative of chaperone activity. In vivo, PDILT forms a tissue-specific chaperone complex with the calnexin homologue calmegin. The identification of a redox-inactive chaperone partnership defines a new system of testis-specific protein folding with implications for male fertility.
ISSN:1059-1524
1939-4586
DOI:10.1091/mbc.E07-02-0147