ArticleFEBS letters2016
The aliphatic chain of cholesterol modulates bilayer interleaflet coupling and domain registration.
Article in FEBS letters, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed.
- Is cholesterol both the lock and key to abnormal transmembrane signals in Autism Spectrum Disorder?Lipids in health and disease · 2024Article
- RAS GTPases and Interleaflet Coupling in the Plasma Membrane.Cold Spring Harbor perspectives in biology · 2023Review
- Computational Modeling of Realistic Cell Membranes.Chemical reviews · 2019Review
- Understanding Membrane Domain-Partitioning Thermodynamics of Transmembrane Domains with Potential of Mean Force Calculations.The journal of physical chemistry. B · 2019Article
- Cholesterol Flip-Flop Impacts Domain Registration in Plasma Membrane Models.The journal of physical chemistry letters · 2018Article
- Microscopic view of lipids and their diverse biological functions.Current opinion in structural biology · 2018Review
- Protein Partitioning into Ordered Membrane Domains: Insights from Simulations.Biophysical journal · 2018Article
- Structural determinants and functional consequences of protein affinity for membrane rafts.Nature communications · 2017Article
- Domain Stability in Biomimetic Membranes Driven by Lipid Polyunsaturation.The journal of physical chemistry. B · 2016Article
Corrections and comments
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Authors and funding
5 authors.
Funding
Abstract
Cholesterol is a necessary component and critical regulator of liquid-ordered membrane domains. However, the structural features that determine its unique physicochemical behaviors are not fully understood. In particular, very little is known about the specific functions of the terminal aliphatic chain of cholesterol, as previous studies have focused mainly on the rigid sterol ring structure and its hydroxyl head. In the current work, we used coarse-grained molecular dynamics simulations to investigate the effect of cholesterol aliphatic chain length on the dynamics and structure of coexisting lipid domains. We found that the aliphatic chain has no appreciable effect on phase separation per se, but it significantly affects the rate of cholesterol flip-flop and intermonolayer interaction. These effects are accompanied by changes in domain dynamics, lateral pressure, and interleaflet coupling. Our study provides useful insight into how biological sterols modulate communication between the outer and inner surfaces of the plasma membrane and, therefore, cellular signaling.
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