SYP51 and SYP52 are sorted through the Golgi apparatus and accumulate on TGN compartments and tonoplast. When overexpressed (a condition naturally occurring in pollen tubes) these proteins and especially SYP51, cause an effect that inhibit vacuolar sorting (1; 2). The interference causes an alteration of endocytic compartments that seem to receive material also from a direct ER-to-vacuole pathway. Bioinformatic analysis on network interaction data, allowed us to evidence direct interactions between SNARE proteins and aquaporins that may have a role in the interference mechanism. Aquaporins have an important role in the modification of membranes propriety (3). One interaction between SNARE and aquaporin have already been described involving the Qc-SNARE SYP61, the Qa-SNARE SYP121 and the aquaporin PIP2;7. These proteins physically interact on plasma membrane (4). In our work, we investigated by ratiometric bimolecular fluorescence complementation (rBiFC) approach (5) the in vivo interaction of the Qc SNAREs AtSYP51 and SYP52 with aquaporins apparently able to bypass the Golgi apparatus. These interactions may control Multi-Vesicular-Bodies formation and represents a regulatory mechanism for unconventional vacuolar transport, exocytosis and endocytosis. Essential bibliography: 1. De Benedictis et al. (2013). AtSYP51/52 functions diverge in the post-golgi traffic and differently affect vacuolar sorting. Mol. Plant 6: 916–930. 2. Di Sansebastiano GP (2013) Defining new SNARE functions: the i-SNARE. Front Plant Sci. 2013 Apr 16;4:99. 3. Maeshima M (2001). Tonoplast Transporters: Organization and Function. Annu. Rev. Plant Physiol. 52: 469–497. 4. Hachez et al. (2014). Arabidopsis SNAREs SYP61 and SYP121 coordinate the trafficking of plasma membrane aquaporin PIP2;7 to modulate the cell membrane water permeability. Plant Cell 26: 3132–47. 5. Grefen, C. and Blatt, M.R. (2012). A 2in1 cloning system enables ratiometric bimolecular fluorescence complementation (rBiFC). Biotechniques 53: 311–314.

Non-SNARE role of AtSYP51/52 in unconventional traffic.

BAROZZI, FABRIZIO;DI SANSEBASTIANO, Gian Pietro
2016

Abstract

SYP51 and SYP52 are sorted through the Golgi apparatus and accumulate on TGN compartments and tonoplast. When overexpressed (a condition naturally occurring in pollen tubes) these proteins and especially SYP51, cause an effect that inhibit vacuolar sorting (1; 2). The interference causes an alteration of endocytic compartments that seem to receive material also from a direct ER-to-vacuole pathway. Bioinformatic analysis on network interaction data, allowed us to evidence direct interactions between SNARE proteins and aquaporins that may have a role in the interference mechanism. Aquaporins have an important role in the modification of membranes propriety (3). One interaction between SNARE and aquaporin have already been described involving the Qc-SNARE SYP61, the Qa-SNARE SYP121 and the aquaporin PIP2;7. These proteins physically interact on plasma membrane (4). In our work, we investigated by ratiometric bimolecular fluorescence complementation (rBiFC) approach (5) the in vivo interaction of the Qc SNAREs AtSYP51 and SYP52 with aquaporins apparently able to bypass the Golgi apparatus. These interactions may control Multi-Vesicular-Bodies formation and represents a regulatory mechanism for unconventional vacuolar transport, exocytosis and endocytosis. Essential bibliography: 1. De Benedictis et al. (2013). AtSYP51/52 functions diverge in the post-golgi traffic and differently affect vacuolar sorting. Mol. Plant 6: 916–930. 2. Di Sansebastiano GP (2013) Defining new SNARE functions: the i-SNARE. Front Plant Sci. 2013 Apr 16;4:99. 3. Maeshima M (2001). Tonoplast Transporters: Organization and Function. Annu. Rev. Plant Physiol. 52: 469–497. 4. Hachez et al. (2014). Arabidopsis SNAREs SYP61 and SYP121 coordinate the trafficking of plasma membrane aquaporin PIP2;7 to modulate the cell membrane water permeability. Plant Cell 26: 3132–47. 5. Grefen, C. and Blatt, M.R. (2012). A 2in1 cloning system enables ratiometric bimolecular fluorescence complementation (rBiFC). Biotechniques 53: 311–314.
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Utilizza questo identificativo per citare o creare un link a questo documento: http://hdl.handle.net/11587/413251
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