Curvature-Driven Lipid Sorting in Biomembranes

Callan-Jones, Andrew; Sorre, Benoît; Bassereau, Patricia

doi:10.1101/cshperspect.a004648

Cited by 128 publications

(139 citation statements)

References 79 publications

(113 reference statements)

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“…8). Indeed, in agreement with previous experimental and theoretical studies [19][20][21][22][23][24] , lipid sorting by membrane shape is not efficient when physiological radii are considered and does not correct significantly lipidpacking defects.…”

Section: Discussionsupporting

confidence: 78%

“…ARTICLE Importantly, the computed defect size constant varies linearly with total curvature (Fig. 3c), suggesting that the distribution of lipid-packing defects of a membrane can be interpreted as the translation in molecular terms of a macroscopic parameter, curvature, used in physics to describe membrane elasticity 8,24,41 . Another implication of the linear relationship between the defect size constant and membrane curvature is that fitting the values with a linear regression should give a good estimate of the variations in lipid packing as a function of curvature (caution must be used when extending this analysis to small, nonphysiological and fusion-prone vesicles).…”

Section: Resultsmentioning

confidence: 99%

“…Most lipids are flexible molecules and, through shape adjustment, might minimize unfavourable exposure of their hydrocarbon chains to water. In addition, lipids with noncylindrical shape (for example, lysolipids or diacylglycerols) could distribute non-randomly within regions of different curvature to reduce geometrical mismatches, although the efficiency of such a mechanism has been questioned due to the propensity of lipids to readily mix through the entropic effect [19][20][21][22][23][24] .…”

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confidence: 99%

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A sub-nanometre view of how membrane curvature and composition modulate lipid packing and protein recruitment

et al. 2014

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Two parameters of biological membranes, curvature and lipid composition, direct the recruitment of many peripheral proteins to cellular organelles. Although these traits are often studied independently, it is their combination that generates the unique interfacial properties of cellular membranes. Here, we use a combination of in vivo, in vitro and in silico approaches to provide a comprehensive map of how these parameters modulate membrane adhesive properties. The correlation between the membrane partitioning of model amphipathic helices and the distribution of lipid-packing defects in membranes of different shape and composition explains how macroscopic membrane properties modulate protein recruitment by changing the molecular topography of the membrane interfacial region. Furthermore, our results suggest that the range of conditions that can be obtained in a cellular context is remarkably large because lipid composition and curvature have, under most circumstances, cumulative effects.

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Section: Discussionsupporting

confidence: 78%

Section: Resultsmentioning

confidence: 99%

mentioning

confidence: 99%

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A sub-nanometre view of how membrane curvature and composition modulate lipid packing and protein recruitment

et al. 2014

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“…6E to G). Such regions of high membrane curvature are enriched in lipids that are favorable to vesicle budding and may be preferred sites for UL36p-driven capsid envelopment (80,81). Alternatively, or in addition, the propensity of UL36-null HSV capsids to form clusters in the cytoplasm (41) might be shared by these membranedocked capsids; in the absence of UL36p, capsids on the organellar surface might associate with one another, forming bright GFPfluorescent foci on the dye-stained membranes and giving rise to the higher Pearson value particles that we observe.…”

Section: Discussionmentioning

confidence: 99%

Herpes Simplex Virus Capsid-Organelle Association in the Absence of the Large Tegument Protein UL36p

Kharkwal

Furgiuele

Smith

et al. 2015

J Virol

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UL36p (VP1/2) is the largest protein encoded by herpes simplex virus 1 (HSV-1) and resides in the innermost layer of the viral tegument, lying between the capsid and the envelope. UL36p performs multiple functions in the HSV life cycle, including an essential role in cytoplasmic envelopment. We earlier described the isolation of a virion-associated cytoplasmic membrane fraction from HSV-infected cells. Biochemical and ultrastructural analyses showed that the organelles in this buoyant fraction contain enveloped infectious HSV particles in their lumens and naked capsids docked to their cytoplasmic surfaces. These organelles can also recruit molecular motors and transport their cargo virions along microtubules in vitro. Here we examine the properties of these HSV-associated organelles in the absence of UL36p. We find that while capsid envelopment is clearly defective, a subpopulation of capsids nevertheless still associate with the cytoplasmic faces of these organelles. The existence of these capsidmembrane structures was confirmed by subcellular fractionation, immunocytochemistry, lipophilic dye fluorescence microscopy, thin-section electron microscopy, and correlative light and electron microscopy. We conclude that capsid-membrane binding can occur in the absence of UL36p and propose that this association may precede the events of UL36p-driven envelopment. IMPORTANCEMembrane association and envelopment of the HSV capsid are essential for the assembly of an infectious virion. Envelopment involves the complex interplay of a large number of viral and cellular proteins; however, the function of most of them is unknown. One example of this is the viral protein UL36p, which is clearly essential for envelopment but plays a poorly understood role. Here we demonstrate that organelles utilized for HSV capsid envelopment still accumulate surface-bound capsids in the absence of UL36p. We propose that UL36p-independent binding of capsids to organelles occurs prior to the function of UL36p in capsid envelopment. Herpesviruses replicate their genomes and assemble DNApackaged capsids in the cell nucleus. It is then generally accepted that capsids bud into the inner nuclear membrane to generate primary enveloped perinuclear virions that subsequently fuse with the outer nuclear membrane, releasing mature nucleocapsids ("naked" capsids) into the cytoplasm (1-3). These naked cytoplasmic capsids subsequently undergo secondary envelopment at a postnuclear organelle to assemble the mature, infectious virion (4-9). Completion of cytoplasmic envelopment requires the coordinated interaction of multiple virally encoded proteins (8,(10)(11)(12)(13) and the participation of components of the cellular endosomal sorting complexes required for transport (ESCRT) machinery (14-19).UL36p (VP1/2) is the largest structural protein encoded by the herpesviridae (20, 21). It is a major constituent of the innermost layer of tegument, the complex protein layer between the capsid and the inner surface of the envelope, and connects the capsid to m...

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“…The exact PL composition varies with cell type and does not simply reflect the PL composition of the PM or the raft and non-raft domains contained therein. Due to differences in PL molecular shape and charge, lateral domains containing different molecular species can form in a membrane due to variations in local curvature (150,151). Thus, the PM PL molecules will be sorted to form the highly curved exovesiculated domain created by ABCA1 activity (Fig.…”

Section: Characterization Of Nascent Hdlmentioning

confidence: 99%