Proteolytic processing of QSOX1A ensures efficient secretion of a potent disulfide catalyst

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
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:Bulleid, Professor Neil and Rudolf, Dr Jana and Pringle, Mrs Marie
Authors: Rudolf, J., Pringle, M., and Bulleid, N.
College/School:College of Medical Veterinary and Life Sciences > Institute of Molecular Cell and Systems Biology
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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Project CodeAward NoProject NamePrincipal InvestigatorFunder's NameFunder RefLead Dept
528621Regulating the redox conditions within the mammalian endoplasmic reticulumNeil BulleidWellcome Trust (WELLCOME)088053/Z/08/ARI MOLECULAR CELL & SYSTEMS BIOLOGY