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Plasma membrane localization of Solanum tuberosum remorin from group 1, homolog 3 is mediated by conformational changes in a novel C-terminal anchor and required for the restriction of potato virus X movement

hal.structure.identifierLaboratoire de biogenèse membranaire [LBM]
dc.contributor.authorPERRAKI, Artemis
hal.structure.identifierLaboratoire de biogenèse membranaire [LBM]
dc.contributor.authorCACAS, Jean-Luc
hal.structure.identifierGembloux Agro-Bio Tech [Faculté universitaire des sciences agronomiques de Gembloux] [[FUSAGx]]
dc.contributor.authorCROWET, Jean-Marc
hal.structure.identifierGembloux Agro-Bio Tech [Faculté universitaire des sciences agronomiques de Gembloux] [[FUSAGx]]
dc.contributor.authorLINS, Laurence
hal.structure.identifierMicrobiologie Fondamentale et Pathogénicité [MFP]
dc.contributor.authorCASTROVIEJO, Michel
hal.structure.identifierBiologie du fruit et pathologie [BFP]
dc.contributor.authorGERMAN-RETANA, Sylvie
hal.structure.identifierLaboratoire de biogenèse membranaire [LBM]
dc.contributor.authorMONGRAND, Sébastien
hal.structure.identifierLaboratoire de biogenèse membranaire [LBM]
hal.structure.identifierJohn Innes Centre [Norwich]
dc.contributor.authorRAFFAELE, Sylvain
dc.date.issued2012-10
dc.identifier.issn0032-0889
dc.description.abstractEnThe formation of plasma membrane (PM) microdomains plays a crucial role in the regulation of membrane signaling and trafficking. Remorins are a plant-specific family of proteins organized in six phylogenetic groups, and Remorins of group 1 are among the few plant proteins known to specifically associate with membrane rafts. As such, they are valuable to understand the molecular bases for PM lateral organization in plants. However, little is known about the structural determinants underlying the specific association of group 1 Remorins with membrane rafts. We used a structure-function approach to identify a short C-terminal anchor (RemCA) indispensable and sufficient for tight direct binding of potato (Solanum tuberosum) REMORIN 1.3 (StREM1.3) to the PM. RemCA switches from unordered to alpha-helical structure in a nonpolar environment. Protein structure modeling indicates that RemCA folds into a tight hairpin of amphipathic helices. Consistently, mutations reducing RemCA amphipathy abolished StREM1.3 PM localization. Furthermore, RemCA directly binds to biological membranes in vitro, shows higher affinity for Detergent-Insoluble Membranes lipids, and targets yellow fluorescent protein to Detergent-Insoluble Membranes in vivo. Mutations in RemCA resulting in cytoplasmic StREM1.3 localization abolish StREM1.3 function in restricting potato virus X movement. The mechanisms described here provide new insights on the control and function of lateral segregation of plant PM.
dc.description.sponsorshipLipides du plasmalemme et signalisation des interactions biotiques chez les végétaux - ANR-09-BLAN-0242
dc.language.isoen
dc.publisherOxford University Press ; American Society of Plant Biologists
dc.rights.urihttp://creativecommons.org/licenses/by/
dc.title.enPlasma membrane localization of Solanum tuberosum remorin from group 1, homolog 3 is mediated by conformational changes in a novel C-terminal anchor and required for the restriction of potato virus X movement
dc.typeArticle de revue
dc.identifier.doi10.1104/pp.112.200519
dc.subject.halSciences du Vivant [q-bio]/Biologie végétale/Phytopathologie et phytopharmacie
dc.description.sponsorshipEuropeManipulation of host target by the AvrBlb2 effector of the late blight pathogen Phytophthora infestans
bordeaux.journalPlant Physiology
bordeaux.page624-637
bordeaux.volume160
bordeaux.issue2
bordeaux.peerReviewedoui
hal.identifierhal-02648092
hal.version1
hal.popularnon
hal.audienceInternationale
hal.origin.linkhttps://hal.archives-ouvertes.fr//hal-02648092v1
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