Project Details
Elucidating the function of the deubiquitinating enzyme AMSH3 in cellular trafficking in Arabidopsis thaliana
Applicant
Professorin Dr. Erika Isono
Subject Area
Cell Biology
Term
from 2008 to 2015
Project identifier
Deutsche Forschungsgemeinschaft (DFG) - Project number 72025348
Ubiquitination as well as deubiquitination regulate a broad range of cellular processes. AMSH proteins are evolutionarily conserved deubiquitinating enzymes. Human AMSH proteins interact with multiple proteins involved in cellular trafficking and are probably controlling the abundance and stability of plasma membrane localized receptors. Our analysis of the Arabidopsis AtAMSH3 has shown that it is essential for vacuole biogenesis, sorting of soluble cargo to the vacuole and endocytosis. Although AMSH proteins seem to play a critical role in intracellular transport in all organisms investigated so far, only a few interacting proteins have been identified. Combining immunoprecipitation and mass spectrometry analysis, we identified proteins that are either potential interactors or potential substrates of AtAMSH3. The goal of this proposal is (1) to elucidate the role of AtAMSH3 in cellular trafficking in the context of its interacting proteins, (2) to define the region in AtAMSH3 responsible for its K48 specificity, and (3) to investigate the chain type specific substrates of AtAMSH3. In carrying out the proposed project, we will contribute to the goals of the SPP (1) by identifying novel UbF-modified proteins, (2) by defining the regulatory functions of these modifications, and (3) by identifying the cellular machineries for UbF deconjugation.
DFG Programme
Priority Programmes