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MBC in Press, published online ahead of print May 16, 2007
Mol. Biol. Cell 10.1091/mbc.E07-02-0147

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Submitted on February 20, 2007
Revised on April 23, 2007
Accepted on May 4, 2007

A Developmentally Regulated Chaperone Complex for the ER of Male Haploid Germ Cells

Marcel van Lith,* Anna-Riikka Karala,{dagger} Dave Bown,* John A. Gatehouse,* Lloyd W. Ruddock,{dagger} Philippa T.K. Saunders,{ddagger} and Adam M. Benham*

*Department of Biological and Biomedical Sciences, University of Durham, Durham, DH1 3LE, United Kingdom; {dagger}Biocenter Oulu and Department of Biochemistry, University of Oulu, 90014 Oulu, Finland; {ddagger}Medical Research Council Human Reproductive Sciences Unit, The Queen’s Medical Research Institute, Edinburgh, EH16 4TJ, United Kingdom

Monitoring Editor: Sean Munro

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 {Delta}-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.

Address correspondence to: Adam M. Benham (adam.benham{at}durham.ac.uk)






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