discovery of a gatekeeper residue in the c-terminal tail of the extracellular signal-regulated protein kinase 5 (erk5)

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ID: 146669
2020
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Abstract
The extracellular signal-regulated protein kinase 5 (ERK5) is a non-redundant mitogen-activated protein kinase (MAPK) that exhibits a unique C-terminal extension which comprises distinct structural and functional properties. Here, we sought to elucidate the significance of phosphoacceptor sites in the C-terminal transactivation domain of ERK5. We have found that Thr732 acted as a functional gatekeeper residue controlling C-terminal-mediated nuclear translocation and transcriptional enhancement. Consistently, using a non-bias quantitative mass spectrometry approach, we demonstrated that phosphorylation at Thr732 conferred selectivity for binding interactions of ERK5 with proteins related to chromatin and RNA biology, whereas a number of metabolic regulators were associated with full-length wild type ERK5. Additionally, our proteomic analysis revealed that phosphorylation of the Ser730-Glu-Thr732-Pro motif could occur independently of dual phosphorylation at Thr218-Glu-Tyr220 in the activation loop. Collectively, our results firmly establish the significance of C-terminal phosphorylation in regulating ERK5 function. The post-translational modification of ERK5 on its C-terminal tail might be of particular relevance in cancer cells where ERK5 has be found to be hyperphosphoryated.
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pearson2020internationaldiscovery Use this key to autocite in the manuscript while using SciMatic Manuscript Manager or Thesis Manager
Authors ;Adam J. Pearson;Paul Fullwood;Gabriela Toro Tapia;Ian Prise;Michael P. Smith;Qiuping Xu;Allan Jordan;Emanuele Giurisato;Alan J. Whitmarsh;Chiara Francavilla;Cathy Tournier
Journal Intertax
Year 2020
DOI
10.3390/ijms21030929
URL
https://www.mdpi.com/1422-0067/21/3/929
Keywords
Mass spectrometry Proteomics phosphorylation mapk

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