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JNK1ß1 is phosphorylated during expression in E. coli and in vitro by MKK4 at three identical novel sites

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dc.contributor.author Owen, GR
dc.contributor.author Stoychev, Stoyan H
dc.contributor.author Achilonu, I
dc.contributor.author Dirr, HW
dc.date.accessioned 2014-07-22T07:45:48Z
dc.date.available 2014-07-22T07:45:48Z
dc.date.issued 2013-03
dc.identifier.citation Owen, G.R, Stoychev, S, Achilonu, I and Dirr, H.W. 2013. JNK1ß1 is phosphorylated during expression in E. coli and in vitro by MKK4 at three identical novel sites. Biochemical and Biophysical Research Communications, vol. 432(4), pp 683-688 en_US
dc.identifier.issn 0006-291X
dc.identifier.uri http://ac.els-cdn.com/S0006291X13002635/1-s2.0-S0006291X13002635-main.pdf?_tid=64f6e920-10d1-11e4-bac7-00000aacb35d&acdnat=1405945405_90a7634dedc5b0129b85683c54c493aa
dc.identifier.uri http://hdl.handle.net/10204/7520
dc.identifier.uri DOI: 10.1016/j.bbrc.2013.02.018
dc.identifier.uri https://www.sciencedirect.com/science/article/pii/S0006291X13002635?via%3Dihub
dc.description Copyright: 2013 Elsevier. This is the pre/post print version. The definitive version is published in Biochemical and Biophysical Research Communications, vol. 432(4), pp 683-688 en_US
dc.description.abstract JNK1 is activated by phosphorylation of the canonical T183 and Y185 residues, modifications that are catalysed typically by the upstream eukaryotic kinases MKK4 and MKK7. Nonetheless, the exact sites at which the most abundant JNK variant, JNK1ß1, is further modified by MKK4 for phospho-regulation has not been previously investigated. Aiming to characterise the nature of JNK1ß1 phosphorylation by active MKK4 using mass spectrometry, a recognized yet uncharacterised phospho-site (S377) as well as two novel phospho-residues (T228 and S284) were identified. Interestingly, the identical sites were phosphorylated during overexpression of JNK1ß1 in E. coli, raising important questions that have significant implications for heterologous protein expression. en_US
dc.language.iso en en_US
dc.publisher Elsevier en_US
dc.relation.ispartofseries Workflow;11883
dc.subject Biochemical research en_US
dc.subject Biophysical research en_US
dc.subject c-Jun N-terminal kinases en_US
dc.subject JNKs en_US
dc.subject Mitogen activated protein kinases en_US
dc.subject MAPKs en_US
dc.title JNK1ß1 is phosphorylated during expression in E. coli and in vitro by MKK4 at three identical novel sites en_US
dc.type Article en_US
dc.identifier.apacitation Owen, G., Stoychev, S. H., Achilonu, I., & Dirr, H. (2013). JNK1ß1 is phosphorylated during expression in E. coli and in vitro by MKK4 at three identical novel sites. http://hdl.handle.net/10204/7520 en_ZA
dc.identifier.chicagocitation Owen, GR, Stoyan H Stoychev, I Achilonu, and HW Dirr "JNK1ß1 is phosphorylated during expression in E. coli and in vitro by MKK4 at three identical novel sites." (2013) http://hdl.handle.net/10204/7520 en_ZA
dc.identifier.vancouvercitation Owen G, Stoychev SH, Achilonu I, Dirr H. JNK1ß1 is phosphorylated during expression in E. coli and in vitro by MKK4 at three identical novel sites. 2013; http://hdl.handle.net/10204/7520. en_ZA
dc.identifier.ris TY - Article AU - Owen, GR AU - Stoychev, Stoyan H AU - Achilonu, I AU - Dirr, HW AB - JNK1 is activated by phosphorylation of the canonical T183 and Y185 residues, modifications that are catalysed typically by the upstream eukaryotic kinases MKK4 and MKK7. Nonetheless, the exact sites at which the most abundant JNK variant, JNK1ß1, is further modified by MKK4 for phospho-regulation has not been previously investigated. Aiming to characterise the nature of JNK1ß1 phosphorylation by active MKK4 using mass spectrometry, a recognized yet uncharacterised phospho-site (S377) as well as two novel phospho-residues (T228 and S284) were identified. Interestingly, the identical sites were phosphorylated during overexpression of JNK1ß1 in E. coli, raising important questions that have significant implications for heterologous protein expression. DA - 2013-03 DB - ResearchSpace DP - CSIR KW - Biochemical research KW - Biophysical research KW - c-Jun N-terminal kinases KW - JNKs KW - Mitogen activated protein kinases KW - MAPKs LK - https://researchspace.csir.co.za PY - 2013 SM - 0006-291X T1 - JNK1ß1 is phosphorylated during expression in E. coli and in vitro by MKK4 at three identical novel sites TI - JNK1ß1 is phosphorylated during expression in E. coli and in vitro by MKK4 at three identical novel sites UR - http://hdl.handle.net/10204/7520 ER - en_ZA


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