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.

Variation in membrane trafficking linked to SNARE AtSYP51 interaction with aquaporin NIP1;1 / Barozzi F.; Papadia P.; Stefano G.; Renna L.; Brandizzi F.; Migoni D.; Fanizzi F.P.; Piro G.; Di Sansebastiano G.-P.. - In: FRONTIERS IN PLANT SCIENCE. - ISSN 1664-462X. - ELETTRONICO. - 9:(2019), pp. 0-0. [10.3389/fpls.2018.01949]

Variation in membrane trafficking linked to SNARE AtSYP51 interaction with aquaporin NIP1;1

Stefano G.;Renna L.;
2019

Abstract

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.
2019
9
0
0
Goal 3: Good health and well-being for people
Barozzi F.; Papadia P.; Stefano G.; Renna L.; Brandizzi F.; Migoni D.; Fanizzi F.P.; Piro G.; Di Sansebastiano G.-P.
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Utilizza questo identificatore per citare o creare un link a questa risorsa: https://hdl.handle.net/2158/1209434
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