Endosomally Localized RGLG-Type E3 RING-Finger Ligases Modulate Sorting of Ubiquitylation-Mimic PIN2

Intracellular sorting and the abundance of sessile plant plasma membrane proteins are imperative for sensing and responding to environmental inputs. A key determinant for inducing adjustments in protein localization and hence functionality is their reversible covalent modification by the small prote...

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Bibliographic Details
Published in:International journal of molecular sciences 2022-06, Vol.23 (12), p.6767
Main Authors: Retzer, Katarzyna, Moulinier-Anzola, Jeanette, Lugsteiner, Rebecca, Konstantinova, Nataliia, Schwihla, Maximilian, Korbei, Barbara, Luschnig, Christian
Format: Article
Language:English
Subjects:
Catalytic activity
Compartments
Genes
Homeostasis
Intracellular
Kinases
Localization
Lysine
Membrane proteins
Membrane Proteins - metabolism
Membrane trafficking
Membranes
Morphogenesis
Plasma
plasma membrane protein
protein stability
Protein Transport
Proteins
Ubiquitin
Ubiquitin - metabolism
ubiquitin E3 ligase
Ubiquitin-Protein Ligases - metabolism
Ubiquitination
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Summary:Intracellular sorting and the abundance of sessile plant plasma membrane proteins are imperative for sensing and responding to environmental inputs. A key determinant for inducing adjustments in protein localization and hence functionality is their reversible covalent modification by the small protein modifier ubiquitin, which is for example responsible for guiding proteins from the plasma membrane to endosomal compartments. This mode of membrane protein sorting control requires the catalytic activity of E3 ubiquitin ligases, amongst which members of the RING DOMAIN LIGASE (RGLG) family have been implicated in the formation of lysine 63-linked polyubiquitin chains, serving as a prime signal for endocytic vacuolar cargo sorting. Nevertheless, except from some indirect implications for such RGLG activity, no further evidence for their role in plasma membrane protein sorting has been provided so far. Here, by employing RGLG1 reporter proteins combined with assessment of plasma membrane protein localization in a loss-of-function mutant, we demonstrate a role for RGLGs in cargo trafficking between plasma membrane and endosomal compartments. Specifically, our findings unveil a requirement for RGLG1 association with endosomal sorting compartments for fundamental aspects of plant morphogenesis, underlining a vital importance for ubiquitylation-controlled intracellular sorting processes.
ISSN:1422-0067
1661-6596
1422-0067
DOI:10.3390/ijms23126767