title: 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].
abstract: The 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 α-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.
authors.affiliation: Centre National de la Recherche Scientifique, Université de Bordeaux, 33076 Bordeaux cedex, France.
authors.forename: Artemis
authors.initials: A
authors.lastname: Perraki
authors.forename: Jean-Luc
authors.initials: JL
authors.lastname: Cacas
authors.forename: Jean-Marc
authors.initials: JM
authors.lastname: Crowet
authors.forename: Laurence
authors.initials: L
authors.lastname: Lins
authors.forename: Michel
authors.initials: M
authors.lastname: Castroviejo
authors.forename: Sylvie
authors.initials: S
authors.lastname: German-Retana
authors.forename: Sébastien
authors.initials: S
authors.lastname: Mongrand
authors.forename: Sylvain
authors.initials: S
authors.lastname: Raffaele
mesh_terms: D016960:Agrobacterium tumefaciens / Q000235:genetics / Q000378:metabolism; D002352:Carrier Proteins / Q000235:genetics / Q000378:metabolism*; D002462:Cell Membrane / Q000235:genetics / Q000378:metabolism* / Q000821:virology; D002942:Circular Dichroism; D003001:Cloning, Molecular; D057927:Hydrophobic and Hydrophilic Interactions; D008051:Lipid Bilayers / Q000378:metabolism; D021962:Membrane Microdomains / Q000235:genetics / Q000378:metabolism; D008565:Membrane Proteins / Q000235:genetics / Q000378:metabolism; D008954:Models, Biological; D009154:Mutation; D010750:Phosphoproteins / Q000235:genetics / Q000378:metabolism*; D010935:Plant Diseases / Q000821:virology; D018515:Plant Leaves / Q000235:genetics / Q000378:metabolism / Q000821:virology; D010940:Plant Proteins / Q000235:genetics / Q000378:metabolism*; D017863:Potexvirus / Q000378:metabolism* / Q000472:pathogenicity; D011485:Protein Binding; D017510:Protein Folding; D017433:Protein Structure, Secondary; D021381:Protein Transport; D011198:Solanum tuberosum / Q000235:genetics / Q000378:metabolism* / Q000821:virology; D013329:Structure-Activity Relationship
chemical_list: D002352:Carrier Proteins; D008051:Lipid Bilayers; D008565:Membrane Proteins; D010750:Phosphoproteins; D010940:Plant Proteins; C103794:remorin