IBBEA   24401
INSTITUTO DE BIODIVERSIDAD Y BIOLOGIA EXPERIMENTAL Y APLICADA
Unidad Ejecutora - UE
congresos y reuniones científicas
Título:
The function of Group 1 REMORINs, proteins that localize to plasma membrane nanodomains, is regulated by phosphorylation during viral infection.
Autor/es:
GERMAIN V., PERRAKI A., GRONNIER J., GERMAN-RETANA S., BAYER E., ZELADA A., MONGRAND S.
Lugar:
Bordeaux
Reunión:
Simposio; 6th European Symposium on Plant lipids; 2013
Resumen:
2013 6th European Symposium on Plant lipids The function of Group 1 REMORINs, proteins that localize to plasma membrane nanodomains, is regulated by phosphorylation during viral infection. Germain V., Perraki A., Gronnier J., German-Retana S., Bayer E., Zelada A., Mongrand S. The group1 Remoirn (REM) proteins are major proteins foud into plasmalemma nanodomains enriched in sphingolipids and sterols, and thus can be considered as planta nanodomains markers (Rafaelle et al., 2009; Demir et al., 2013). There is evidence that REM protein phosphorylation is potentiallly involved in early signalling and defense aginst bioagressors. Group1 REM were reported in different plant species to be phosphorylated in response to treatment like oligogañacturonides, the general elicitor Fñf22, and in response to Pseudomona syrinage (Farmer et al., 1198; Benshop et al., 2007, Widjaja et al., 2009) but the function of REM phosphorylarion remains largerly unknown. In previous work, we showed that StREM1.3 from potato palys a role in the viral propagation of the Potato virus X (PVX), a member of Potexvirus, a widespread genus of agronomically important RNA viruses. Funstional analyses in transgenci tomato over- or under-expressing REM have clearly demonstarted an antagonostic correlation bettween the level of the REM protein and the local and systemic spread PVX (Rafaelle et al., 2009). The same effect on viral propagation has been also found in Nicotiana benthamiana transgenic lines overexpressing REM. IN thsi work, we investigated the role of REM phosphorylation during the PVX infection in Nicotiana benthamiana leaves. In vitro biochemical analyses showed that the amount of phosphorylated recombinant REM in increased in the presence of microsomes isolated from PVX ifected issues. This suggests that the activity of a membrane-associated kinase is increased in response to viral infection. The physiological consequences of REM phosphorylationis currently tested by analysing the PVX movement in leaves transiently expressing different phosphomutants. The work is focusing on different aspects essential to viral propagation including plasmodesmata gating and inhibition of host postranscriptional gene silencing. Preliminary results were also obtained on the kinase characterization. Taken all together, these data should give new insights on the function of the host protein REM and more generally of nanodomains, for PVX widespread and how this process is regulated by REM post-translational modifications.