Dr Ojore Oka
- Research Fellow (Molecular Biosciences)
telephone:
0141 3306453
email:
Ojore.Oka@glasgow.ac.uk
Lab 232, Institute of MC&SB, Davidson Building, Glasgow G12 8QQ
Publications
2022
Oka, O. B. V. , Pierre, A. S., Pringle, M. A. , Tungkum, W., Cao, Z., Fleming, B. and Bulleid, N. J. (2022) Activation of the UPR sensor ATF6α is regulated by its redox-dependent dimerization and ER retention by ERp18. Proceedings of the National Academy of Sciences of the United States of America, 119(12), e2122657119. (doi: 10.1073/pnas.2122657119) (PMID:35286189) (PMCID:PMC8944254)
2020
Cao, X., Lilla, S., Cao, Z., Pringle, M. A., Oka, O. B.V. , Robinson, P. J. , Szmaja, T., Van Lith, M., Zanivan, S. and Bulleid, N. (2020) The mammalian cytosolic thioredoxin reductase pathway acts via a membrane 1 protein to reduce ER-localised proteins. Journal of Cell Science, 133, jcs241976. (doi: 10.1242/jcs.241976) (PMID:32184267) (PMCID:PMC7197872)
2019
Oka, O. B.V. , van Lith, M., Rudolf, J., Tungkum, W., Pringle, M.-A. and Bulleid, N. J. (2019) ERp18 regulates the activation of ATF6α during the unfolded protein response. EMBO Journal, 2019, e100990. (doi: 10.15252/embj.2018100990) (PMID:31209066)
2018
Biddau, M. et al. (2018) Two essential Thioredoxins mediate apicoplast biogenesis, protein import, and gene expression in Toxoplasma gondii. PLoS Pathogens, 14(2), e1006836. (doi: 10.1371/journal.ppat.1006836) (PMID:29470517) (PMCID:PMC5823475)
2017
Poet, G. J., Oka, O. B.V. , Van Lith, M., Cao, Z., Robinson, P. J. , Pringle, M. A. , Arnér, E. S.J. and Bulleid, N. (2017) Cytosolic thioredoxin reductase 1 is required for correct disulfide formation in the ER. EMBO Journal, 36(5), pp. 693-702. (doi: 10.15252/embj.201695336) (PMID:28093500) (PMCID:PMC5331760)
2015
Oka, O. , Yeoh, H. and Bulleid, N. (2015) Thiol-disulfide exchange between the PDI family of oxidoreductases negates the requirement for an oxidase or reductase for each enzyme. Biochemical Journal, 469(2), pp. 279-288. (doi: 10.1042/BJ20141423) (PMID:25989104) (PMCID:PMC4613490))
2014
Shepherd, C., Oka, O. B. V. and Bulleid, N. J. (2014) Inactivation of mammalian Ero 1α is catalysed by specific protein disulfide isomerases. Biochemical Journal, 461(1), pp. 107-113. (doi: 10.1042/BJ20140234) (PMID:24758166) (PMCID:PMC4243250)
2013
Oka, O. B. V. , Pringle, M. A. , Schopp, I. M., Braakman, I. and Bulleid, N. J. (2013) ERdj5 is the ER reductase that catalyzes the removal of non-native disulfides and correct folding of the LDL receptor. Molecular Cell, 50(6), pp. 793-804. (doi: 10.1016/j.molcel.2013.05.014)
Oka, O. B.V. and Bulleid, N. J. (2013) Forming disulfides in the endoplasmic reticulum. Biochimica et Biophysica Acta: Molecular Cell Research, 1833(11), pp. 2425-2429. (doi: 10.1016/j.bbamcr.2013.02.007)
2010
Chambers, J.E., Tavender, T.J., Oka, O.B.V. , Warwood, S., Knight, D. and Bulleid, N.J. (2010) The reduction potential of the active site disulfides of human protein disulfide isomerase limits oxidation of the enzyme by Ero1. Journal of Biological Chemistry, 285(38), pp. 29200-29207. (doi: 10.1074/jbc.M110.156596)
Articles
Oka, O. B. V. , Pierre, A. S., Pringle, M. A. , Tungkum, W., Cao, Z., Fleming, B. and Bulleid, N. J. (2022) Activation of the UPR sensor ATF6α is regulated by its redox-dependent dimerization and ER retention by ERp18. Proceedings of the National Academy of Sciences of the United States of America, 119(12), e2122657119. (doi: 10.1073/pnas.2122657119) (PMID:35286189) (PMCID:PMC8944254)
Cao, X., Lilla, S., Cao, Z., Pringle, M. A., Oka, O. B.V. , Robinson, P. J. , Szmaja, T., Van Lith, M., Zanivan, S. and Bulleid, N. (2020) The mammalian cytosolic thioredoxin reductase pathway acts via a membrane 1 protein to reduce ER-localised proteins. Journal of Cell Science, 133, jcs241976. (doi: 10.1242/jcs.241976) (PMID:32184267) (PMCID:PMC7197872)
Oka, O. B.V. , van Lith, M., Rudolf, J., Tungkum, W., Pringle, M.-A. and Bulleid, N. J. (2019) ERp18 regulates the activation of ATF6α during the unfolded protein response. EMBO Journal, 2019, e100990. (doi: 10.15252/embj.2018100990) (PMID:31209066)
Biddau, M. et al. (2018) Two essential Thioredoxins mediate apicoplast biogenesis, protein import, and gene expression in Toxoplasma gondii. PLoS Pathogens, 14(2), e1006836. (doi: 10.1371/journal.ppat.1006836) (PMID:29470517) (PMCID:PMC5823475)
Poet, G. J., Oka, O. B.V. , Van Lith, M., Cao, Z., Robinson, P. J. , Pringle, M. A. , Arnér, E. S.J. and Bulleid, N. (2017) Cytosolic thioredoxin reductase 1 is required for correct disulfide formation in the ER. EMBO Journal, 36(5), pp. 693-702. (doi: 10.15252/embj.201695336) (PMID:28093500) (PMCID:PMC5331760)
Oka, O. , Yeoh, H. and Bulleid, N. (2015) Thiol-disulfide exchange between the PDI family of oxidoreductases negates the requirement for an oxidase or reductase for each enzyme. Biochemical Journal, 469(2), pp. 279-288. (doi: 10.1042/BJ20141423) (PMID:25989104) (PMCID:PMC4613490))
Shepherd, C., Oka, O. B. V. and Bulleid, N. J. (2014) Inactivation of mammalian Ero 1α is catalysed by specific protein disulfide isomerases. Biochemical Journal, 461(1), pp. 107-113. (doi: 10.1042/BJ20140234) (PMID:24758166) (PMCID:PMC4243250)
Oka, O. B. V. , Pringle, M. A. , Schopp, I. M., Braakman, I. and Bulleid, N. J. (2013) ERdj5 is the ER reductase that catalyzes the removal of non-native disulfides and correct folding of the LDL receptor. Molecular Cell, 50(6), pp. 793-804. (doi: 10.1016/j.molcel.2013.05.014)
Oka, O. B.V. and Bulleid, N. J. (2013) Forming disulfides in the endoplasmic reticulum. Biochimica et Biophysica Acta: Molecular Cell Research, 1833(11), pp. 2425-2429. (doi: 10.1016/j.bbamcr.2013.02.007)
Chambers, J.E., Tavender, T.J., Oka, O.B.V. , Warwood, S., Knight, D. and Bulleid, N.J. (2010) The reduction potential of the active site disulfides of human protein disulfide isomerase limits oxidation of the enzyme by Ero1. Journal of Biological Chemistry, 285(38), pp. 29200-29207. (doi: 10.1074/jbc.M110.156596)
Grants
Grants and Awards listed are those received whilst working with the University of Glasgow.
- Identification and validation of ATF6 protein interaction partners during cell stress
Wellcome Trust
2016 - 2016