Remorin, a plant phosphorylated Protein located in Sphingolipid-enriched Membrane rafts, incvolved in virus propagation.

PERRAKI A., GRONNIER J., BAYER E., MECCHIA M., BINAGHI M., GERMAN-RETANA S., ZELADA A. GERMAIN V. AND MONGRAND S

Bordeaux

Simposio; 6th European Symposium on Plant lipids; 2013

6th European Symposium on Plant lipids Remorin, a plant phosphorylated Protein located in Sphingolipid-enriched Membrane rafts, involved in virus propagation. Perraki A., Gronnier J., Bayer E., Mecchia M., Binaghi M., German-Retana S. Zelada A. Germain V. and Mongrand S. The Remorin (REM) proteins are plant-specific oligomeric proteins that have been reported to localize to the plasma membrane raft microdomain enriched in sterol and sphingolipids, despite their overall hydrophilic nature (Perraki et al., 2012). There is evidence that the REM protein phosphorylation is potentially implicated in the early signaling and defense.Benschop et al. (2007) detected teh AtREM1.3 (group 1b of REM protein family) to be phosphorylated in response to treatment with the general elicitor flg22, while the Widjaja et al. (2008) suggested that the phosphorylation of AtREM1.2 is potentially implicated in early signalling upon infection with Pseudomonas syringae. The precise exact function of the group 1 REM protein phosphorylation remains unknown. Beside, we showed that Potato virus X (PX) movement is inversely related to poatto StREM 1.3 accumulation and that StREM1.3 can interact physically with the movement protein TRIPLE GENE BLOCK PROTEIN1 from PVX. In this work, we studied the role og TGBp1/StREM1.3 interactionand the phosphorylation of REM in presence of virus. The physiological consequence of this interaction and phosphorylation, virus spreading, postranscriptional gene silencing, plasmodesmata gating, size exclusion limit, kinase activation were studied. The role of the raft microdomain mobilization of REM during virus infection will be particularly discussed.