Variation in Membrane Trafficking Linked to SNARE AtSYP51 Interaction With Aquaporin NIP1;1
| Autor: | Federica Brandizzi, Francesco Paolo Fanizzi, Luciana Renna, Fabrizio Barozzi, Giovanni Stefano, Gian Pietro Di Sansebastiano, Gabriella Piro, Paride Papadia, Danilo Migoni |
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| Přispěvatelé: | Barozzi, Fabrizio, Papadia, Paride, Stefano, Giovanni, Renna, Luciana, Brandizzi, Federica, Migoni, Danilo, Fanizzi, Francesco Paolo, Piro, Gabriella, DI SANSEBASTIANO, Gian Pietro |
| Jazyk: | angličtina |
| Rok vydání: | 2019 |
| Předmět: |
0106 biological sciences
0301 basic medicine Aquaporin Vacuole Plant Science lcsh:Plant culture 01 natural sciences Interactome tonoplast recycling 03 medical and health sciences chemistry.chemical_compound symbols.namesake NIP1 Arabidopsis thaliana lcsh:SB1-1110 Arsenite Original Research biology Endoplasmic reticulum Membrane transport Golgi apparatus biology.organism_classification tonoplast Cell biology aquaporin endoplasmic reticulum 030104 developmental biology chemistry SNARE SYP51 symbols rBiFC 010606 plant biology & botany |
| Zdroj: | Frontiers in Plant Science, Vol 9 (2019) Frontiers in Plant Science |
| ISSN: | 1664-462X |
| DOI: | 10.3389/fpls.2018.01949 |
| Popis: | SYP51 and 52 are the two members of the SYP5 Qc-SNARE gene family in Arabidopsis thaliana. These two proteins, besides their high level of sequence identity (85%), have shown to have differential functional specificity and possess a different interactome. Here we describe a unique and specific interaction of SYP51 with an ER aquaporin, AtNIP1;1 (also known as NLM1) indicated to be able to transport arsenite [As(III)] and previously localized on PM. In the present work we investigate in detail such localization in vivo and characterize the interaction with SYP51. We suggest that this interaction may reveal a new mechanism regulating tonoplast invagination and recycling. We propose this interaction to be part of a regulatory mechanism associated with direct membrane transport from ER to tonoplast and Golgi mediated vesicle trafficking. We also demonstrate that NIP1;1 is important for plant tolerance to arsenite but does not alter its uptake or translocation. To explain such phenomenon the hypothesis that SYP51/NIP1;1 interaction modifies ER and vacuole ability to accumulate arsenite is discussed. |
| Databáze: | OpenAIRE |
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