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| 1 | TOLs Function as Ubiquitin Receptors in the Early Steps of the ESCRT Pathway in Higher Plants显示文摘Protein abundance and localization at the plasma membrane(PM)shapes plant development and mediates adaptation to changing environmental conditions.It is regulated by ubiquitination,a post-translational modification crucial for the proper sorting of endocytosed PM proteins to the vacuole for subsequent degradation.To understand the significance and the variety of roles played by this reversible modification,the function of ubiquitin receptors,which translate the ubiquitin signature into a cellular response,needs to be elucidated.In this study,we show that TOL(TOM1-like)proteins function in plants as multivalent ubiquitin receptors,governing ubiquitinated cargo delivery to the vacuole via the conserved Endosomal Sorting Complex Required for Transport(ESCRT)pathway.TOL2 and TOL6 interact with components of the ESCRT machinery and bind to K63-linked ubiquitin via two tandemly arranged conserved ubiquitin-binding domains.Mutation of these domains results not only in a loss of ubiquitin binding but also altered localization,abolishing TOL6 ubiquitin receptor activity.Function and localization of TOL6 is itself regulated by ubiquitination,whereby TOL6 ubiquitination potentially modulates degradation of PM-localized cargoes,assisting in the fine-tuning of the delicate interplay between protein recycling and downregulation.Taken together,our findings demonstrate the function and regulation of a ubiquitin receptor that mediates vacuolar degradation of PM proteins in higher plants. | Jeanette Moulinier-Anzola Maximilian Schwihla Lucinda De-Araujo Christina Artner Lisa Jorg Nataliia Konstantinova Christian Luschnig Barbara Korbei | 2020 | Molecular Plant2020，13，5： | 3 |
| 2 | Plasma Membrane Protein Ubiquitylation and Degradation as Determinants of Positional Growth in Plants显示文摘Being sessile organisms,plants evolved an unparalleled plasticity in their post‐embryonic development,allowing them to adapt and fne‐tune their vital parameters to an ever‐changing environment.Crosstalk between plants and their environment requires tight regulation of information exchange at the plasma membrane(PM).Plasma membrane proteins mediate such communication,by sensing variations in nutrient availability,external cues as well as by controlled solute transport across the membrane border.Localization and steady‐state levels are essential for PM protein function and ongoing research identifed cis‐and trans‐acting determinants,involved in control of plant PM protein localization and turnover.In this overview,we summarize recent progress in our understanding of plant PM protein sorting and degradation via ubiquitylation,a post‐translational and reversible modifcation of proteins.We highlight characterized components of the machinery involved in sorting of ubiquitylated PM proteins and discuss consequences of protein ubiquitylation on fate of selected PM proteins.Specifcally,we focus on the role of ubiquitylation and PM protein degradation in the regulation of polar auxin transport(PAT).We combine this regulatory circuit with further aspects of PM protein sorting control,to address the interplay of events that might control PAT and polarized growth in higher plants. | Barbara Korbei Christian Luschnig | 2013 | Journal of Integrative Plant Biology2013，55，9： | 3 |
| 3 | Lamina-associated polypeptide 2 alpha binds intranuclear A-type lamins显示文摘 | Dechat T Korbei B Vaughan OA | | 0，，19： | 1 |
| 4 | Seizure susceptibility and locus eeruleus activation are reduced'following environmental en- richment in an animal model of epilepsy 显示文摘 | Korbey SM Heiurichs SC Leussis MP | 2008 | Epilepsy & Behavior2008，12，1： | 1 |
| 5 | Seizure susceptibility and locus ceruleus activation are reduced following environmental enrichment in an animal model of epilepsy 显示文摘 | Korbey S M Heinrichs S C Leussis M P | 2008 | Epilepsy & Behavior2008，12，1： | 1 |
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