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Differential function of TOL homologs

Differential function of TOL homologs

Barbara Korbei (ORCID: 0000-0002-0439-0435)
  • Grant DOI 10.55776/P33989
  • Funding program Principal Investigator Projects
  • Status ended
  • Start January 1, 2021
  • End December 31, 2025
  • Funding amount € 397,971

Disciplines

Biology (100%)

Keywords

    Arabidopsis thaliana, Ubiquitin receptor, Endocytosis, ESCRT, Plasma Membrane Protein Degradation

Abstract

Climate change, which manifests itself in harsher environmental conditions, has put the food supply of a growing world population under considerable pressure. Since plants cannot simply move away from an unfavorable environment by themselves, they have developed intricate mechanisms in order to be able to react quickly and precisely to their surroundings (adaptation). The plasma membrane of a cell is the interface between the inside and the outside and is interspersed with proteins that are essential for the detection and transmission of internal and external stimuli. Strict control of the amount and positioning of these proteins is critical for adaptive processes. In the model plant Arabidopsis thaliana, we have shown that a protein family, the TOL proteins, is responsible for the initial steps in the transport of plasma membrane proteins to the vacuole for their degradation. In this project we want to investigate the function of individual members of this protein family in regulating the abundance of plasma membrane proteins in various signaling pathways. In addition to their general role in the degradation pathway of membrane proteins, individual TOLs can play a more specific role in different signaling pathways. One example is the role of distinct TOLs in the signaling pathway of the plant hormone abscisic acid, which plays an important role in germination and drought stress. Evidence that TOLs fulfill these differential functions comes from the analysis of their domains, their diverse expression patterns and their subcellular localizations. TOLs also appear to undergo dynamic rearrangements in response to certain environmental stimuli. The main aim of this project is to evaluate which networks and signal pathways the TOLs are involved in and to identify differences in their localization and their relevant interaction partners. In summary, these experiments should provide insights into the first steps in the degradation of plasma membrane proteins relevant in essential signaling pathways. This basic research project will establish previously unknown regulatory processes in the control of protein turnover at the plasma membrane. This will contribute to our understanding of how plants optimize and fine-tune their response to the constantly changing environment. Furthermore, results from the model plant Arabidopsis thaliana can be translated to assist in the generation of crops, which are more resilient to the harsher climate of the future.

Research institution(s)
  • Universität für Bodenkultur Wien - 100%
Project participants
  • Christian Luschnig, Universität für Bodenkultur Wien , national collaboration partner
  • Eva Stöger, Universität für Bodenkultur Wien , national collaboration partner
International project participants
  • Daniel Van Damme, Ghent University - Belgium
  • Jürgen Kleine-Vehn, Albert-Ludwigs-Universität Freiburg - Germany

Research Output

  • 62 Citations
  • 3 Publications
Publications
  • 2022
    Title Endosomally Localized RGLG-Type E3 RING-Finger Ligases Modulate Sorting of Ubiquitylation-Mimic PIN2
    DOI 10.3390/ijms23126767
    Type Journal Article
    Author Retzer K
    Journal International Journal of Molecular Sciences
    Pages 6767
    Link Publication
  • 2022
    Title Ubiquitination of the ubiquitin-binding machinery: how early ESCRT components are controlled
    DOI 10.1042/ebc20210042
    Type Journal Article
    Author Korbei B
    Journal Essays in Biochemistry
    Pages 169-177
    Link Publication
  • 2021
    Title Auxin and Root Gravitropism: Addressing Basic Cellular Processes by Exploiting a Defined Growth Response
    DOI 10.3390/ijms22052749
    Type Journal Article
    Author Konstantinova N
    Journal International Journal of Molecular Sciences
    Pages 2749
    Link Publication

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