Rudolf, J., Pringle, M. and Bulleid, N. (2013) Proteolytic processing of QSOX1A ensures efficient secretion of a potent disulfide catalyst. Biochemical Journal, 2013(454), pp. 181-190. (doi: 10.1042/BJ20130360)
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Abstract
QSOX1 (quiescin sulfhydryl oxidase 1) efficiently catalyses the insertion of disulfide bonds into a wide range of proteins. The enzyme is mechanistically well characterized, but its subcellular location and the identity of its protein substrates remain ill-defined. The function of QSOX1 is likely to involve disulfide formation in proteins entering the secretory pathway or outside the cell. In the present study, we show that this enzyme is efficiently secreted from mammalian cells despite the presence of a transmembrane domain. We identify internal cleavage sites and demonstrate that the protein is processed within the Golgi apparatus to yield soluble enzyme. As a consequence of this efficient processing, QSOX1 is probably functional outside the cell. Also, QSOX1 forms a dimer upon cleavage of the C-terminal domain. The processing of QSOX1 suggests a novel level of regulation of secretion of this potent disulfide catalyst and producer of hydrogen peroxide.
| Item Type: | Articles |
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| Additional Information: | The final version of record is available at http://www.biochemj.org/bj/default.htm |
| Status: | Published |
| Refereed: | Yes |
| Glasgow Author(s) Enlighten ID: | Rudolf, Dr Jana and Bulleid, Professor Neil and Pringle, Mrs Marie |
| Authors: | Rudolf, J., Pringle, M., and Bulleid, N. |
| College/School: | College of Medical Veterinary and Life Sciences > School of Molecular Biosciences |
| Journal Name: | Biochemical Journal |
| Publisher: | Portland Press Ltd. |
| ISSN: | 0264-6021 |
| ISSN (Online): | 1470-8728 |
| Copyright Holders: | Copyright © 2013 The Authors |
| First Published: | First published in Biochemical Journal 2013(454):181-190 |
| Publisher Policy: | Reproduced under a Creative Commons License |
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