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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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Autores principales: Retzer, Katarzyna, Moulinier-Anzola, Jeanette, Lugsteiner, Rebecca, Konstantinova, Nataliia, Schwihla, Maximilian, Korbei, Barbara, Luschnig, Christian
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2022
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9224344/
https://www.ncbi.nlm.nih.gov/pubmed/35743207
http://dx.doi.org/10.3390/ijms23126767
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author Retzer, Katarzyna
Moulinier-Anzola, Jeanette
Lugsteiner, Rebecca
Konstantinova, Nataliia
Schwihla, Maximilian
Korbei, Barbara
Luschnig, Christian
author_facet Retzer, Katarzyna
Moulinier-Anzola, Jeanette
Lugsteiner, Rebecca
Konstantinova, Nataliia
Schwihla, Maximilian
Korbei, Barbara
Luschnig, Christian
author_sort Retzer, Katarzyna
collection PubMed
description 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 rglg1 rglg2 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.
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spelling pubmed-92243442022-06-24 Endosomally Localized RGLG-Type E3 RING-Finger Ligases Modulate Sorting of Ubiquitylation-Mimic PIN2 Retzer, Katarzyna Moulinier-Anzola, Jeanette Lugsteiner, Rebecca Konstantinova, Nataliia Schwihla, Maximilian Korbei, Barbara Luschnig, Christian Int J Mol Sci Article 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 rglg1 rglg2 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. MDPI 2022-06-17 /pmc/articles/PMC9224344/ /pubmed/35743207 http://dx.doi.org/10.3390/ijms23126767 Text en © 2022 by the authors. https://creativecommons.org/licenses/by/4.0/Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (https://creativecommons.org/licenses/by/4.0/).
spellingShingle Article
Retzer, Katarzyna
Moulinier-Anzola, Jeanette
Lugsteiner, Rebecca
Konstantinova, Nataliia
Schwihla, Maximilian
Korbei, Barbara
Luschnig, Christian
Endosomally Localized RGLG-Type E3 RING-Finger Ligases Modulate Sorting of Ubiquitylation-Mimic PIN2
title Endosomally Localized RGLG-Type E3 RING-Finger Ligases Modulate Sorting of Ubiquitylation-Mimic PIN2
title_full Endosomally Localized RGLG-Type E3 RING-Finger Ligases Modulate Sorting of Ubiquitylation-Mimic PIN2
title_fullStr Endosomally Localized RGLG-Type E3 RING-Finger Ligases Modulate Sorting of Ubiquitylation-Mimic PIN2
title_full_unstemmed Endosomally Localized RGLG-Type E3 RING-Finger Ligases Modulate Sorting of Ubiquitylation-Mimic PIN2
title_short Endosomally Localized RGLG-Type E3 RING-Finger Ligases Modulate Sorting of Ubiquitylation-Mimic PIN2
title_sort endosomally localized rglg-type e3 ring-finger ligases modulate sorting of ubiquitylation-mimic pin2
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9224344/
https://www.ncbi.nlm.nih.gov/pubmed/35743207
http://dx.doi.org/10.3390/ijms23126767
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