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Mol Biol Cell. 2007 Aug;18(8):2795-804. Epub 2007 May 16.

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

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  • 1Department of Biological and Biomedical Sciences, University of Durham, Durham, DH1 3LE, United Kingdom.

Abstract

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.

PMID:
17507649
[PubMed - indexed for MEDLINE]
PMCID:
PMC1949379
Free PMC Article

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