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

By M. van Lith, A. Karala, D. Bown, J. Gatehouse, L. Ruddock, P Saunders and A. M. Benham

Abstract

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

Publisher: American Society for Cell Biology
Year: 2007
DOI identifier: 10.1091/mbc.E07-02-0147
OAI identifier: oai:dro.dur.ac.uk.OAI2:3659
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