ArticleBiomacromolecules2019
Cooperation of Helix Insertion and Lateral Pressure to Remodel Membranes.
Article in Biomacromolecules, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed.
- Membrane Association of Intrinsically Disordered Proteins.Annual review of biophysics · 2025Review
- Protein-membrane interactions: sensing and generating curvature.Trends in biochemical sciences · 2024Review
- Quantitative Seed Amplification Assay: A Proof-of-Principle Study.The journal of physical chemistry. B · 2023Article
- Remodeling of the Plasma Membrane by Surface-Bound Protein Monomers and Oligomers: The Critical Role of Intrinsically Disordered Regions.The Journal of membrane biology · 2022Review
- Insights into Membrane Curvature Sensing and Membrane Remodeling by Intrinsically Disordered Proteins and Protein Regions.The Journal of membrane biology · 2022Review
- Interactions between SARS-CoV-2 N-Protein and α-Synuclein Accelerate Amyloid Formation.ACS chemical neuroscience · 2022Article
- Spiers Memorial Lecture: Analysis andFaraday discussions · 2021Article
- In situ kinetic measurements of α-synuclein aggregation reveal large population of short-lived oligomers.PloS one · 2021Article
- Biophysical forces in membrane bending and traffic.Current opinion in cell biology · 2020Review
- Deep mutational scanning reveals the structural basis for α-synuclein activity.Nature chemical biology · 2020Article
- Kinetics of Histidine-Tagged Protein Association to Nickel-Decorated Liposome Surfaces.Langmuir : the ACS journal of surfaces and colloids · 2019Article
- Protein Amphipathic Helix Insertion: A Mechanism to Induce Membrane Fission.Frontiers in cell and developmental biology · 2019Review
Corrections and comments
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Authors and funding
5 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Nature has developed different protein mediated mechanisms to remodel cellular membranes. One of the proteins that is implicated in these processes is α-synuclein (αS). Here we investigate if besides αS's membrane bound amphipathic helix the disordered, solvent exposed tail of the protein contributes to membrane reshaping. We produced αS variants with elongated or truncated disordered solvent exposed domains. We observe a transformation of opaque multi lamellar vesicle solutions into nonscattering solutions containing smaller structures upon addition of all αS variants. Experimental data combined with model calculations show that the cooperation of helix insertion and lateral pressure exerted by the disordered domain makes the full length protein decidedly more efficient in membrane remodeling than the truncated version. Using disordered domains may not only be cost-efficient, it may also add a new level of control over vesicle fusion/fission by expansion or compaction of the domain.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.