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Lipid Selectivity, Orientation, and Extent of Membrane Binding of Nonacylated RP2

dc.contributor.authorDEMERS, Eric
dc.contributor.authorBOISSELIER, Elodie
dc.contributor.authorHORCHANI, Habib
dc.contributor.authorBLAUDEZ, Daniel
dc.contributor.authorCALVEZ, Philippe
dc.contributor.authorCANTIN, Line
dc.contributor.authorBELLEY, Nicolas
dc.contributor.authorCHAMPAGNE, Sophie
dc.contributor.authorDESBAT, Bernard
dc.contributor.authorSALESSE, Christian
dc.date.accessioned2020-09-03T08:02:13Z
dc.date.available2020-09-03T08:02:13Z
dc.date.issued2015
dc.identifier.issn0006-2960
dc.identifier.urihttps://oskar-bordeaux.fr/handle/20.500.12278/10991
dc.description.abstractEnRetinitis pigmentosa 2 (RP2) is an ubiquitary protein of 350 residues. The N-terminus of RP2 contains putative sites of myristoylation and palmitoylation. The dually acylated protein is predominantly localized to the plasma membrane. However, clinically occurring substitution mutations of RP2 in photoreceptors lead to the expression of a nonacylated protein, which was shown to be misrouted to intracellular organelles using different cell lines. However, the parameters responsible for the modulation of the membrane binding of nonacylated RP2 (naRP2) are still largely unknown. The maximal insertion pressure of naRP2 has thus been determined after its injection into the subphase underneath monolayers of phospholipids, which are typical of photoreceptor membranes. These data demonstrated that naRP2 shows a preferential binding to saturated phospholipid monolayers. Moreover, polarization modulation infrared reflection absorption spectroscopy has allowed comparison of the secondary structure of this protein in solution and upon binding to phospholipid monolayers. In addition, simulations of these spectra have allowed to determine that the beta-helix of naRP2 has an orientation of 60 degrees with respect to the normal, which remains unchanged regardless of the type of phospholipid. Finally, ellipsometric measurements of naRP2 demonstrated that its particular affinity for saturated phospholipids can be explained by its larger extent of insertion in this phospholipid monolayer compared to that in polyunsaturated phospholipid monolayers.
dc.language.isoen
dc.title.enLipid Selectivity, Orientation, and Extent of Membrane Binding of Nonacylated RP2
dc.typeArticle de revue
dc.identifier.doi10.1021/bi501517r
dc.subject.halChimie/Matériaux
bordeaux.journalBiochemistry
bordeaux.page2560-2570
bordeaux.volume54
bordeaux.hal.laboratoriesInstitut de Chimie & de Biologie des Membranes & des Nano-objets (CBMN) - UMR 5248*
bordeaux.hal.laboratoriesInstitut de Chimie & de Biologie des Membranes & des Nano-objets (CBMN, UMR 5248)
bordeaux.issue16
bordeaux.institutionUniversité de Bordeaux
bordeaux.institutionBordeaux INP
bordeaux.COinSctx_ver=Z39.88-2004&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.jtitle=Biochemistry&rft.date=2015&rft.volume=54&rft.issue=16&rft.spage=2560-2570&rft.epage=2560-2570&rft.eissn=0006-2960&rft.issn=0006-2960&rft.au=DEMERS,%20Eric&BOISSELIER,%20Elodie&HORCHANI,%20Habib&BLAUDEZ,%20Daniel&CALVEZ,%20Philippe&rft.genre=article


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