Endocytosis of BRASSINOSTEROID INSENSITIVE1 Is Partly Driven by a Canonical Tyr-Based Motif
| Autor: | Isabelle Vanhoutte, Eugenia Russinova, Lucas Alves Neubus Claus, Rajesh Kumar, Peng Wang, Wei Siao, Daniël Van Damme, Jiří Friml, Derui Liu, Xiuyang Zhao, Grégory Vert, Alexander W. Johnson, Klaas Yperman, Sara Martins, Kyle W. Bender |
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| Přispěvatelé: | Universiteit Gent = Ghent University (UGENT), Center for Plant Systems Biology (PSB Center), Vlaams Instituut voor Biotechnologie [Ghent, Belgique] (VIB), Institute of Science and Technology [Klosterneuburg, Austria] (IST Austria), University of Illinois at Urbana-Champaign [Urbana], University of Illinois System, Laboratoire de Recherche en Sciences Végétales (LRSV), Université Toulouse III - Paul Sabatier (UT3), Université de Toulouse (UT)-Université de Toulouse (UT)-Centre National de la Recherche Scientifique (CNRS), Signalisation Cellulaire et Ubiquitination, Université de Toulouse (UT)-Université de Toulouse (UT)-Centre National de la Recherche Scientifique (CNRS)-Université Toulouse III - Paul Sabatier (UT3), European Project: 1009584(2010), Universiteit Gent = Ghent University [Belgium] (UGENT), Institute of Science and Technology [Austria] (IST Austria), Université Fédérale Toulouse Midi-Pyrénées-Université Fédérale Toulouse Midi-Pyrénées-Centre National de la Recherche Scientifique (CNRS), Université Fédérale Toulouse Midi-Pyrénées-Université Fédérale Toulouse Midi-Pyrénées-Centre National de la Recherche Scientifique (CNRS)-Université Toulouse III - Paul Sabatier (UT3) |
| Jazyk: | angličtina |
| Rok vydání: | 2020 |
| Předmět: |
POLAR LOCALIZATION
0106 biological sciences 0301 basic medicine ADAPTER COMPLEX Endocytic cycle Amino Acid Motifs MESH: Cell Membrane / metabolism Arabidopsis Plant Science 01 natural sciences chemistry.chemical_compound MESH: Amino Acid Motifs MESH: Endocytosis / physiology Internalization media_common MESH: Arabidopsis / metabolism TYROSINE PHOSPHORYLATION biology Signal transducing adaptor protein CLATHRIN-MEDIATED ENDOCYTOSIS ARABIDOPSIS Plants Genetically Modified Endocytosis Cell biology MESH: Arabidopsis Proteins / genetics FACTOR RECEPTOR MESH: Protein Domains MESH: Arabidopsis / genetics EPIDERMAL-GROWTH-FACTOR CELLULOSE SYNTHASE MESH: Mutation SORTING SIGNALS media_common.quotation_subject Green Fluorescent Proteins [SDV.BC]Life Sciences [q-bio]/Cellular Biology Clathrin In Brief 03 medical and health sciences MESH: Arabidopsis Proteins / metabolism Protein Domains MESH: Arabidopsis Proteins / chemistry Kinase activity MESH: Protein Kinases / chemistry Arabidopsis Proteins Cell Membrane fungi Biology and Life Sciences Tyrosine phosphorylation Cell Biology Receptor-mediated endocytosis MESH: Protein Kinases / genetics MESH: Protein Kinases / metabolism 030104 developmental biology chemistry MESH: Plants Genetically Modified MESH: Tyrosine / chemistry Mutation biology.protein Tyrosine MESH: Green Fluorescent Proteins / genetics Protein Kinases STRUCTURAL EXPLANATION 010606 plant biology & botany |
| Zdroj: | The Plant cell The Plant cell, 2020, 32 (11), pp.3598-3612. ⟨10.1105/tpc.20.00384⟩ The Plant cell, American Society of Plant Biologists (ASPB), 2020, 32 (11), pp.3598-3612. ⟨10.1105/tpc.20.00384⟩ The Plant Cell Plant Cell PLANT CELL |
| ISSN: | 1040-4651 1532-298X |
| Popis: | Clathrin-mediated endocytosis (CME) and its core endocytic machinery are evolutionarily conserved across all eukaryotes. In mammals, the heterotetrameric adaptor protein complex-2 (AP-2) sorts plasma membrane (PM) cargoes into vesicles via the recognition of motifs based on Tyr or di-Leu in their cytoplasmic tails. However, in plants, very little is known about how PM proteins are sorted for CME and whether similar motifs are required. In Arabidopsis (Arabidopsis thaliana), the brassinosteroid (BR) receptor BR INSENSITIVE1 (BRI1) undergoes endocytosis, which depends on clathrin and AP-2. Here, we demonstrate that BRI1 binds directly to the medium AP-2 subunit (AP2M). The cytoplasmic domain of BRI1 contains five putative canonical surface-exposed Tyr-based endocytic motifs. The Tyr-to-Phe substitution in Y898KAI reduced BRI1 internalization without affecting its kinase activity. Consistently, plants carrying the BRI1Y898F mutation were hypersensitive to BRs. Our study demonstrates that AP-2–dependent internalization of PM proteins via the recognition of functional Tyr motifs also operates in plants. |
| Databáze: | OpenAIRE |
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