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  1. IPB Halle
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    • Trenner 0
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Dissmeyer, N.; Coux, O.; Rodriguez, M. S.; Barrio, R.; the Core Group Members of PROTEOSTASIS, .; PROTEOSTASIS: A European Network to Break Barriers and Integrate Science on Protein Homeostasis Trends Biochem. Sci. 44 383-387 (2019) DOI: 10.1016/j.tibs.2019.01.007
  • Abstract
  • BibText
  • RIS

Protein homeostasis (proteostasis) is at the core of cellular functions. The European network PROTEOSTASIS was created to steer research and foster collaborations in the interconnected fields of posttranslational modifications by ubiquitin family members and protein turnover by proteasome, autophagy, and lysosomal systems in health and diseases, across the kingdoms of life.

Publications

Dissmeyer, N.; Conditional Protein Function via N-Degron Pathway–Mediated Proteostasis in Stress Physiology Annu. Rev. Plant Biol. 70 83-117 (2019) DOI: 10.1146/annurev-arplant-050718-095937
  • Abstract
  • BibText
  • RIS

The N-degron pathway, formerly the N-end rule pathway, regulates functions of regulatory proteins. It impacts protein half-life and therefore directs the actual presence of target proteins in the cell. The current concept holds that the N-degron pathway depends on the identity of the amino (N)-terminal amino acid and many other factors, such as the follow-up sequence at the N terminus, conformation, flexibility, and protein localization. It is evolutionarily conserved throughout the kingdoms. One possible entry point for substrates of the N-degron pathway is oxidation of N-terminal Cys residues. Oxidation of N-terminal Cys is decisive for further enzymatic modification of various neo–N termini by arginylation that generates potentially neofunctionalized or instable proteoforms. Here, I focus on the posttranslational modifications that are encompassed by protein degradation via the Cys/Arg branch of the N-degron pathway—part of the PROTEOLYSIS 6 (PRT6)/N-degron pathway—as well as the underlying physiological principles of this branch and its biological significance in stress response.

Publications

Dissmeyer, N.; Graciet, E.; Holdsworth, M. J.; Gibbs, D. J.; N-term 2017: Proteostasis via the N-terminus Trends Biochem. Sci. 44 293-295 (2019) DOI: 10.1016/j.tibs.2017.11.006
  • Abstract
  • BibText
  • RIS

N-term 2017 was the first international meeting to bring together researchers from diverse disciplines with a shared interest in protein N-terminal modifications and the N-end rule pathway of ubiquitin-mediated proteolysis, providing a platform for interdisciplinary cross-kingdom discussions and collaborations, as well as strengthening the visibility of this growing scientific community.

Publications

Bäumler, J.; Riber, W.; Klecker, M.; Müller, L.; Dissmeyer, N.; Weig, A. R.; Mustroph, A.; AtERF#111/ABR1 is a transcriptional activator involved in the wounding response Plant J. 100 969-990 (2019) DOI: 10.1111/tpj.14490
  • Abstract
  • BibText
  • RIS

AtERF#111/ABR1 belongs to the group X of the ERF/AP2 transcription factor family (GXERFs) and is shoot specifically induced under submergence and hypoxia. It was described to be an ABA‐response repressor, but our data reveal a completely different function. Surprisingly, AtERF#111 expression is strongly responsive to wounding stress. Expression profiling of ERF#111‐overexpressing (OE) plants, which show morphological phenotypes like increased root hair length and number, strengthens the hypothesis of AtERF#111 being involved in the wounding response, thereby acting as a transcriptional activator of gene expression. Consistent with a potential function outside of oxygen signalling, we could not assign AtERF#111 as a target of the PRT6 N‐degron pathway, even though it starts with a highly conserved N‐terminal Met−Cys (MC) motif. However, the protein is unstable as it is degraded in an ubiquitin‐dependent manner. Finally, direct target genes of AtERF#111 were identified by microarray analyses and subsequently confirmed by protoplast transactivation assays. The special roles of diverse members of the plant‐specific GXERFs in coordinating stress signalling and wound repair mechanisms have been recently hypothesized, and our data suggest that AtERF#111 is indeed involved in these processes.

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