Preparation of Liposomes That Mimic the Membrane of Endoplasmic Reticulum of Rat Hepatocytes

Watanabe, Jun; Asaka, Youko; Mino, Kazuto; Kanamura, Shinsuke

doi:10.1093/oxfordjournals.jmicro.a023429

Cited by 5 publications

(4 citation statements)

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“…A mixture of lipids composed of 59% 1,2-Dioleoyl-sn-Glycero-3-Phosphocholine (DOPC), 18% 1,2-Dioleoyl-sn-Glycero-3-Phosphoethanolamine (DOPE), 3% 1,2-Dioleoyl-sn-Glycero-3-[Phospho-L-Serine] (Sodium salt) (DOPS), mimicking the lipid-composition the endoplasmic reticulum [36], doped with 20% {1,2,-dioleoyl-sn-glycero-3-[(N-(5-amino-1-carboxypntyl) iminodiacetic acid) succinyl]}-nitrilotriacetic acid-Ni 2+ (DOGS-NTA-Ni) was used. The lipid-dissolving organic solvent was completely dried under gentle flow of nitrogen and then the lipid mixture was solubilised by adding the protein storage buffer containing 4% (w/v) n-octyl-β-D-glucoside.…”

Section: Methodsmentioning

confidence: 99%

Membrane Remodeling by the Double-Barrel Scaffolding Protein of Poxvirus

et al. 2011

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In contrast to most enveloped viruses, poxviruses produce infectious particles that do not acquire their internal lipid membrane by budding through cellular compartments. Instead, poxvirus immature particles are generated from atypical crescent-shaped precursors whose architecture and composition remain contentious. Here we describe the 2.6 Å crystal structure of vaccinia virus D13, a key structural component of the outer scaffold of viral crescents. D13 folds into two jellyrolls decorated by a head domain of novel fold. It assembles into trimers that are homologous to the double-barrel capsid proteins of adenovirus and lipid-containing icosahedral viruses. We show that, when tethered onto artificial membranes, D13 forms a honeycomb lattice and assembly products structurally similar to the viral crescents and immature particles. The architecture of the D13 honeycomb lattice and the lipid-remodeling abilities of D13 support a model of assembly that exhibits similarities with the giant mimivirus. Overall, these findings establish that the first committed step of poxvirus morphogenesis utilizes an ancestral lipid-remodeling strategy common to icosahedral DNA viruses infecting all kingdoms of life. Furthermore, D13 is the target of rifampicin and its structure will aid the development of poxvirus assembly inhibitors.

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Section: Methodsmentioning

confidence: 99%

Membrane Remodeling by the Double-Barrel Scaffolding Protein of Poxvirus

et al. 2011

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“…We performed additional binding experiments using a shorter peptide derived from Myo19 membrane motif that contains the peak in predicted helix propensity and the corresponding ER mutant (Fig. S4D, Table S2, Myo19 858-883 and Myo19 858-RK882/3SS , respectively) to either OMM or ER mimicking vesicles [20% phosphatidylethanolamine, 66% phosphatidylcholine, 9% phosphatidylinositol, 3% dioleoyl phosphatidylserine (Watanabe et al, 1996)]. Both peptides showed similar affinities to OMMmimicking vesicles (45.0±14.1 and 49.0±17.2 μM for WT or mutant peptide, respectively, Fig.…”

Section: Myo19-derived Peptide Binds To Omm-mimicking Vesiclesmentioning

confidence: 99%

Myo19 is an outer mitochondrial membrane motor and effector of starvation-induced filopodia

Shneyer

Ušaj

Henn

2016

Journal of Cell Science

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Mitochondria respond to environmental cues and stress conditions. Additionally, the disruption of the mitochondrial network dynamics and its distribution is implicated in a variety of neurodegenerative diseases. Here, we reveal a new function for Myo19 in mitochondrial dynamics and localization during the cellular response to glucose starvation. Ectopically expressed Myo19 localized with mitochondria to the tips of starvation-induced filopodia. Corollary to this, RNA interference (RNAi)-mediated knockdown of Myo19 diminished filopodia formation without evident effects on the mitochondrial network. We analyzed the Myo19-mitochondria interaction, and demonstrated that Myo19 is uniquely anchored to the outer mitochondrial membrane (OMM) through a 30-45-residue motif, indicating that Myo19 is a stably attached OMM molecular motor. Our work reveals a new function for Myo19 in mitochondrial positioning under stress.

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“…Synthetic lipid bilayers (liposomes) based on lipid-like small-molecule amphiphiles have been extensively studied. [1][2][3][4] These systems, however, lack functionality in terms of a true mimic of cell surface interactions. The use of click chemistry has been seminal in terms of producing bioconjugates that combine the physical properties of polymers and the specific functionality of peptides and proteins.…”

Section: Introductionmentioning

confidence: 99%