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EnglishThe 12 amino acid peptide derived from the Arabidopsis soluble secretory protein CLAVATA3 (CLV3) acts at the cell surface in a signalling system that regulates the size of apical meristems. The subcellular pathway involved in releasing the peptide from its precursor is unknown. We show that a CLV3-GFP fusion expressed in transfected tobacco protoplasts or transgenic tobacco plants has very short intracellular half-life that cannot be extended by the secretory traffic inhibitors brefeldin A and wortmannin. The fusion is biologically active, since the incubation medium of protoplasts from CLV3-GFP-expressing tobacco contains the CLV3 peptide and inhibits root growth. The rapid disappearance of intact CLV3-GFP requires the signal peptide and is inhibited by the proteasome inhibitor MG132 or coexpression with a mutated CDC48 that inhibits endoplasmic reticulum-associated protein degradation (ERAD). The synthesis of CLV3-GFP is specifically supported by the endoplasmic reticulum cha- perone endoplasmin in an in vivo assay. Our results indicate that processing of CLV3 starts intracellularly in an early compartment of the secretory pathway and that ERAD could play a regulatory or direct role in the active peptide synthesis.
| Titolo: | Expression of CLAVATA3 fusions indicates rapid intracellular processing and a role of ERAD |
| Autore/i: | Francesca De Marchis; Sara Colanero; Eva M. Klein; Davide Mainieri; Viviana M. Prota; Michele Bellucci; Giampiero Pagliuca; Elisa Zironi; Teresa Gazzotti; Alessandro Vitale; Andrea Pompa |
| Autore/i Unibo: | |
| Anno: | 2018 |
| Rivista: | |
| Digital Object Identifier (DOI): | 10.1016/j.plantsci.2018.03.020 |
| Abstract: | The 12 amino acid peptide derived from the Arabidopsis soluble secretory protein CLAVATA3 (CLV3) acts at the cell surface in a signalling system that regulates the size of apical meristems. The subcellular pathway involved in releasing the peptide from its precursor is unknown. We show that a CLV3-GFP fusion expressed in transfected tobacco protoplasts or transgenic tobacco plants has very short intracellular half-life that cannot be extended by the secretory traffic inhibitors brefeldin A and wortmannin. The fusion is biologically active, since the incubation medium of protoplasts from CLV3-GFP-expressing tobacco contains the CLV3 peptide and inhibits root growth. The rapid disappearance of intact CLV3-GFP requires the signal peptide and is inhibited by the proteasome inhibitor MG132 or coexpression with a mutated CDC48 that inhibits endoplasmic reticulum-associated protein degradation (ERAD). The synthesis of CLV3-GFP is specifically supported by the endoplasmic reticulum cha- perone endoplasmin in an in vivo assay. Our results indicate that processing of CLV3 starts intracellularly in an early compartment of the secretory pathway and that ERAD could play a regulatory or direct role in the active peptide synthesis. |
| Data stato definitivo: | 2019-06-03T16:54:25Z |
| Appare nelle tipologie: | 1.01 Articolo in rivista |
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| File | Descrizione | Tipo | Licenza | |
|---|---|---|---|---|
| De Marchis et al. 2018_postprint.pdf | Post-print | Licenza per Accesso Aperto. Creative Commons Attribuzione - Non commerciale - Non opere derivate 4.0 (CCBYNCND) | Open Access Visualizza/Apri | |
| 1-s2.0-S016894521731066X-mmc1.pptx | File Supplementare | Licenza per Accesso Aperto. Creative Commons Attribuzione - Non commerciale - Non opere derivate 4.0 (CCBYNCND) | Open Access Visualizza/Apri | |
| 1-s2.0-S016894521731066X-mmc2.pptx | File Supplementare | Licenza per Accesso Aperto. Creative Commons Attribuzione - Non commerciale - Non opere derivate 4.0 (CCBYNCND) | Open Access Visualizza/Apri | |
| 1-s2.0-S016894521731066X-mmc3.pptx | File Supplementare | Licenza per Accesso Aperto. Creative Commons Attribuzione - Non commerciale - Non opere derivate 4.0 (CCBYNCND) | Open Access Visualizza/Apri |
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