Lipid map of the mammalian cell

Meer, Gerrit van; Kroon, Anton I.P.M. de

doi:10.1242/jcs.071233

Cited by 575 publications

(487 citation statements)

References 55 publications

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“…Peptides were prepared as 75 mM samples, as structural details at this concentration usually appear very pronounced, yet the samples remain in their liquid phase and do not display gel-like characteristics. Figure 2 reveals that all investigated samples can be roughly divided into three classes: (1) peptides that show no superstructural features, (2) peptides with pronounced lamellar characteristics, including an inter-lamellar structure factor, and (3) one peptide with a combination of lamellar and tape-like characteristics. More precisely, (1) two peptides (V 3 D and V 4 D 2 ) did not self-assemble into ordered structures, even at those high peptide concentrations.…”

Section: Structural Characterization Of Self-assembled Pure Peptide Smentioning

confidence: 99%

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Peptide self-assembly into lamellar phases and the formation of lipid-peptide nanostructures

et al. 2017

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Lipids exhibit an extraordinary polymorphism in self-assembled mesophases, with lamellar phases as the most relevant biological representative. To mimic lipid lamellar phases with amphiphilic designer peptides, seven systematically varied short peptides were engineered. Indeed, four peptide candidates (V 4 D, V 4 WD, V 4 WD 2 , I 4 WD 2 ) readily self-assembled into lamellae in aqueous solution. Small-angle X-ray scattering (SAXS) patterns revealed ordered lamellar structures with a repeat distance of ~ 4-5 nm. Transmission electron microscopy (TEM) images confirmed the presence of stacked sheets. Two derivatives (V 3 D and V 4 D 2 ) remained as loose aggregates dispersed in solution; one peptide (L 4 WD 2 ) formed twisted tapes with internal lamellae and an antiparallel β-type monomer alignment. To understand the interaction of peptides with lipids, they were mixed with phosphatidylcholines. Low peptide concentrations (1.1 mM) induced the formation of a heterogeneous mixture of vesicular structures. Large multilamellar vesicles (MLV, d-spacing ~ 6.3 nm) coexisted with oligo-or unilamellar vesicles (~ 50 nm in diameter) and bicelle-like structures (~ 45 nm length, ~ 18 nm width). High peptide concentrations (11 mM) led to unilamellar vesicles (ULV, diameter ~ 260-280 nm) with a homogeneous mixing of lipids and peptides. SAXS revealed the temperature-dependent fine structure of these ULVs. At 25 °C the bilayer is in a fully interdigitated state (headgroup-to-headgroup distance d HH ~ 2.9 nm), whereas at 50 °C this interdigitation opens up (d HH ~ 3.6 nm). Our results highlight the versatility of self-assembled peptide superstructures. Subtle changes in the amino acid composition are key design elements in creating peptide-or lipidpeptide nanostructures with richness in morphology similar to that of naturally occurring lipids.

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Section: Structural Characterization Of Self-assembled Pure Peptide Smentioning

confidence: 99%

“…The remarkable ability of phospholipids to selfassemble into various lamellar structures is essential for life, as they create the fundamental structural component of biological membranes [1][2][3][4][5]. Lipid-like designer peptides are promising candidates to mimic this feature.…”

Section: Introductionmentioning

confidence: 99%

Peptide self-assembly into lamellar phases and the formation of lipid-peptide nanostructures

et al. 2017

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“…Myo1a bound DOPS-containing liposomes in vitro, and PS is one of the most abundant negatively charged lipid species found in the inner leaflet of the plasma membrane (44,45). Thus, we sought to determine if PS colocalizes with Myo1a-TH1 in microvilli.…”

Section: Myo1a-th1 Interacts With Ps In Brush Bordermentioning

confidence: 99%

“…3F and 7). PS is one of the most abundant phospholipid species found in the inner leaflet of the plasma membrane (44,45) and is therefore a good candidate for supporting electrostatic interactions between Myo1a-TH1 and the microvillar membrane. Although the labeling methods used here show that PS and PI(4,5)P 2 are both found in microvilli, it is still unclear if these lipids compartmentalize into subdomains along the microvillar axis.…”

Section: Dissecting the Membrane Binding Mechanism Of Myo1a-th1-mentioning

confidence: 99%

Myosin-1A Targets to Microvilli Using Multiple Membrane Binding Motifs in the Tail Homology 1 (TH1) Domain

Mazerik

Tyska

2012

Journal of Biological Chemistry

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Background: Myo1a is an abundant membrane binding motor that targets to microvilli in intestinal epithelial cells. Results: Myo1a interacts with acidic phospholipids using distinct motifs at the N and C terminus of the TH1 domain. Conclusion: Membrane binding potential of Myo1a is distributed throughout TH1 rather than localized to a single motif. Significance: Different class I myosins rely on different strategies for targeting to cellular membranes.

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“…Recent lipid profiling has shown that PG has a relatively low abundance with respect to phosphatidylethanolamine (PE) in prokaryotes and either PE or phosphatidylcholine (PC) in eukaryotes [12,13,14]. This suggests that its structural contribution is minimal or controlled tightly.…”

Section: Introductionmentioning

confidence: 99%

Is phosphatidylglycerol essential for terrestrial life?

Furse

2016

J Chem Biol

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Lipids are of increasing importance in understanding biological systems. Lipids carrying an anionic charge are noted in particular for their electrostatic interactions with both proteins and divalent cations. However, the biological, analytical, chemical and biophysical data of such species are rarely considered together, limiting our ability to assess the true role of such lipids in vivo. In this review, evidence from a range of studies about the lipid phosphatidylglycerol is considered. This evidence supports the conclusions that this lipid is ubiquitous in living systems and generally of low abundance but probably fundamental for terrestrial life. Possible reasons for this are discussed and further questions posed.

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Lipid map of the mammalian cell

Cited by 575 publications

References 55 publications

Peptide self-assembly into lamellar phases and the formation of lipid-peptide nanostructures

Peptide self-assembly into lamellar phases and the formation of lipid-peptide nanostructures

Myosin-1A Targets to Microvilli Using Multiple Membrane Binding Motifs in the Tail Homology 1 (TH1) Domain

Is phosphatidylglycerol essential for terrestrial life?

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