Publication details for Dr Adam Benhamvan Lith, M., Karala, A., Bown, D., Gatehouse, J., Ruddock, L., Saunders, P & Benham, AM. (2007). A developmentally regulated chaperone complex for the endoplasmic reticulum of male haploid germ cells. Molecular Biology of the Cell 18(8): 2795-2804.
- Publication type: Journal Article
- ISSN/ISBN: 1059-1524
- DOI: 10.1091/mbc.E07-02-0147
- Further publication details on publisher web site
- Durham Research Online (DRO) - may include full text
Author(s) from Durham
Glycoprotein folding is mediated by lectin-like chaperones and protein disulfide isomerases (PDIs) in the endoplasmic reticulum (ER). 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 post-meiotic 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 -somatostatin and nonnative BPTI 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.