Influenza Virus M2 Protein Mediates ESCRT-Independent Membrane Scission
Jeremy S. Rossman,Jeremy S. Rossman,Xianghong Jing,George P. Leser,Robert A. Lamb,Robert A. Lamb +5 more
TLDR
It is shown that M2 localizes to the neck of budding virions and that mutation of the M2 amphipathic helix results in failure of the virus to undergo membrane scission and virion release, suggesting that M1 mediates the final steps of budding for influenza viruses, bypassing the need for host ESCRT proteins.About:
This article is published in Cell.The article was published on 2010-09-17 and is currently open access. It has received 490 citations till now. The article focuses on the topics: ESCRT & SIN3A.read more
Citations
More filters
Journal ArticleDOI
Coronavirus envelope protein: current knowledge
TL;DR: Data shows that E is involved in critical aspects of the viral life cycle and that CoVs lacking E make promising vaccine candidates, which can aid in the production of effective anti-coronaviral agents for both human CoVs and enzootic CoVs.
Journal ArticleDOI
Membrane Organization and Lipid Rafts
Kai Simons,Julio L. Sampaio +1 more
TL;DR: The emerging principles of membrane architecture are reviewed with special emphasis on lipid organization and domain formation, which combines the potential for sphingolipid-cholesterol self-assembly with protein specificity to focus and regulate membrane bioactivity.
Journal ArticleDOI
Influenza virus assembly and budding.
TL;DR: This review investigates the latest research on influenza virus budding in an attempt to provide a step-by-step analysis of the assembly and budding processes for influenza viruses.
Journal ArticleDOI
Membrane curvature at a glance
TL;DR: Some of the discoveries about the functions of membrane curvature, where in addition to providing cell or organelle shape, local curvature can affect processes like membrane scission and fusion as well as protein concentration and enzyme activation on membranes.
Journal ArticleDOI
Membrane bending by protein-protein crowding
Jeanne C. Stachowiak,Jeanne C. Stachowiak,Eva M. Schmid,Christopher J. Ryan,Hyoung Sook Ann,Darryl Y. Sasaki,Michael B. Sherman,Phillip L. Geissler,Phillip L. Geissler,Daniel A. Fletcher,Daniel A. Fletcher,Carl C. Hayden +11 more
TL;DR: A third general mechanism for bending fluid cellular membranes: protein–protein crowding is proposed, and it is found that even proteins unrelated to membrane curvature, such as green fluorescent protein (GFP), can bend membranes when sufficiently concentrated.
References
More filters
Journal ArticleDOI
Lipid rafts and signal transduction
Kai Simons,Derek Toomre +1 more
TL;DR: It is now becoming clear that lipid micro-environments on the cell surface — known as lipid rafts — also take part in this process of signalling transduction, where protein–protein interactions result in the activation of signalling cascades.
Journal ArticleDOI
Sorting of GPI-anchored proteins to glycolipid-enriched membrane subdomains during transport to the apical cell surface
Deborah A. Brown,John K. Rose +1 more
TL;DR: It is shown that a protein with a glycosylphosphatidyl inositol (GPI) anchor can be recovered from lysates of epithelial cells in a low density, detergent-insoluble form, supporting the model proposed by Simons and colleagues for sorting of certain membrane proteins to the apical surface after intracellular association with glycosphingolipids.
Journal ArticleDOI
Structure and Mechanism of the M2 Proton Channel of Influenza A Virus
Jason R. Schnell,James J. Chou +1 more
TL;DR: The structure of the tetrameric M2 channel in complex with rimantadine, determined by NMR is presented and predicted to counter the effect of drug binding by either increasing the hydrophilicity of the pore or weakening helix–helix packing, thus facilitating channel opening.
Journal ArticleDOI
The actions of melittin on membranes.
TL;DR: Despite the structural complexity of integral membrane proteins, it is interesting that in some respects their study be more straightforward, lacking as they do the elusive properties of melittin which limit the possibility of defining their interaction with membranes in terms of a single conformation, location, orientation and association state within the membrane.
Journal ArticleDOI
Membrane scission by the ESCRT-III complex
TL;DR: Three subunits of ESCRT-III, Vps20, Snf7 and Vps24, are sufficient to detach intralumenal vesicles and are reconstituted and visualized by fluorescence microscopy.
Related Papers (5)
Structure and Mechanism of the M2 Proton Channel of Influenza A Virus
Jason R. Schnell,James J. Chou +1 more