A unifying mechanism accounts for sensing of membrane curvature by BAR domains, amphipathic helices and membrane-anchored proteins

2010 ◽  
Vol 21 (4) ◽  
pp. 381-390 ◽  
Author(s):  
Vikram Kjøller Bhatia ◽  
Nikos S. Hatzakis ◽  
Dimitrios Stamou
Keyword(s):  
Membrane Curvature ◽  
Amphipathic Helices ◽  
Bar Domains

scholarly journals BAR domains, amphipathic helices and membrane-anchored proteins use the same mechanism to sense membrane curvature

FEBS Letters ◽  
2010 ◽  
Vol 584 (9) ◽  
pp. 1848-1855 ◽  
Author(s):  
K.L. Madsen ◽  
V.K. Bhatia ◽  
U. Gether ◽  
D. Stamou
Keyword(s):  
Membrane Curvature ◽  
Amphipathic Helices ◽  
Bar Domains

Spotting Differences in Molecular Dynamic Simulations of Influenza A M2 Protein-Ligand Complexes by Varying M2 construct, Lipid Bilayer and Force Field

2019 ◽  
Author(s):  
Dimitrios Kolokouris ◽  
Iris Kalenderoglou ◽  
Panagiotis Lagarias ◽  
Antonios Kolocouris
Keyword(s):  
Molecular Dynamic ◽  
Lipid Bilayer ◽  
Influenza A ◽  
Md Simulations ◽  
Membrane Curvature ◽  
Buffer Size ◽  
M2 Protein ◽  
Dynamic Simulations ◽  
Amphipathic Helices ◽  
Drug Protein Binding

<p>We studied by molecular dynamic (MD) simulations systems including the inward<sub>closed</sub> state of influenza A M2 protein in complex with aminoadamantane drugs in membrane bilayers. We varied the M2 construct and performed MD simulations in M2TM or M2TM with amphipathic helices (M2AH). We also varied the lipid bilayer by changing either the lipid, DMPC or POPC, POPE or POPC/cholesterol (chol), or the lipids buffer size, 10x10 Å<sup>2 </sup>or 20x20 Å<sup>2</sup>. We aimed to suggest optimal system conditions for the computational description of this ion channel and related systems. Measures performed include quantities that are available experimentally and include: (a) the position of ligand, waters and chlorine anion inside the M2 pore, (b) the passage of waters from the outward Val27 gate of M2 S31N in complex with an aminoadamantane-aryl head blocker, (c) M2 orientation, (d) the AHs conformation and structure which is affected from interactions with lipids and chol and is important for membrane curvature and virus budding. In several cases we tested OPLS2005, which is routinely applied to describe drug-protein binding, and CHARMM36 which describes reliably protein conformation. We found that for the description of the ligands position inside the M2 pore, a 10x10 Å<sup>2</sup> lipids buffer in DMPC is needed when M2TM is used but 20x20 Å<sup>2</sup> lipids buffer of the softer POPC; when M2AH is used all 10x10 Å<sup>2</sup> lipid buffers with any of the tested lipids can be used. For the passage of waters at least M2AH with a 10x10 Å<sup>2</sup> lipid buffer is needed. The folding conformation of AHs which is defined from hydrogen bonding interactions with the bilayer and the complex with chol is described well with a 10x10 Å<sup>2</sup> lipids buffer and CHARMM36. </p>

scholarly journals The Many Faces of Amphipathic Helices

Biomolecules ◽  
2018 ◽  
Vol 8 (3) ◽  
pp. 45 ◽  
Author(s):  
Manuel Giménez-Andrés ◽  
Alenka Čopič ◽  
Bruno Antonny
Keyword(s):  
Lipid Bilayers ◽  
General Scheme ◽  
Membrane Curvature ◽  
Hydrophobic Residues ◽  
Cellular Processes ◽  
Amphipathic Helices ◽  
Polar Residues ◽  
Secondary Feature ◽  
Helical Turn ◽  
The Many

Amphipathic helices (AHs), a secondary feature found in many proteins, are defined by their structure and by the segregation of hydrophobic and polar residues between two faces of the helix. This segregation allows AHs to adsorb at polar–apolar interfaces such as the lipid surfaces of cellular organelles. Using various examples, we discuss here how variations within this general scheme impart membrane-interacting AHs with different interfacial properties. Among the key parameters are: (i) the size of hydrophobic residues and their density per helical turn; (ii) the nature, the charge, and the distribution of polar residues; and (iii) the length of the AH. Depending on how these parameters are tuned, AHs can deform lipid bilayers, sense membrane curvature, recognize specific lipids, coat lipid droplets, or protect membranes from stress. Via these diverse mechanisms, AHs play important roles in many cellular processes.

scholarly journals Membrane Curvature Sensing by Amphipathic Helices

2011 ◽  
Vol 286 (49) ◽  
pp. 42603-42614 ◽  
Author(s):  
Martin Borch Jensen ◽  
Vikram Kjøller Bhatia ◽  
Christine C. Jao ◽  
Jakob Ewald Rasmussen ◽  
Søren L. Pedersen ◽  
...  
Keyword(s):  
Membrane Curvature ◽  
Curvature Sensing ◽  
Amphipathic Helices

scholarly journals Roles of Amphipathic Helices and the Bin/Amphiphysin/Rvs (BAR) Domain of Endophilin in Membrane Curvature Generation

2010 ◽  
Vol 285 (26) ◽  
pp. 20164-20170 ◽  
Author(s):  
Christine C. Jao ◽  
Balachandra G. Hegde ◽  
Jennifer L. Gallop ◽  
Prabhavati B. Hegde ◽  
Harvey T. McMahon ◽  
...  
Keyword(s):  
Membrane Curvature ◽  
Bar Domain ◽  
Amphipathic Helices

scholarly journals F-BAR domains: multifunctional regulators of membrane curvature

2008 ◽  
Vol 121 (12) ◽  
pp. 1951-1954 ◽  
Author(s):  
R. J. W. Heath ◽  
R. H. Insall
Keyword(s):  
Membrane Curvature ◽  
Bar Domains

scholarly journals Screening the Sensing of Membrane Curvature by BAR domains on Single Liposome Arrays

2009 ◽  
Vol 96 (3) ◽  
pp. 570a
Author(s):  
Vikram K. Bhatia ◽  
Kenneth L. Madsen ◽  
Pierre-Yves Bolinger ◽  
Per Hedegârd ◽  
Ulrik Gether ◽  
...  
Keyword(s):  
Membrane Curvature ◽  
Bar Domains

scholarly journals Quantifying Membrane Curvature Generation of Drosophila Amphiphysin N-BAR Domains

2010 ◽  
Vol 1 (23) ◽  
pp. 3401-3406 ◽  
Author(s):  
Michael C. Heinrich ◽  
Benjamin R. Capraro ◽  
Aiwei Tian ◽  
Jose M. Isas ◽  
Ralf Langen ◽  
...  
Keyword(s):  
Membrane Curvature ◽  
Bar Domains

scholarly journals Interplay of septin amphipathic helices in sensing membrane-curvature and filament bundling

2020 ◽  
Author(s):  
Benjamin L. Woods ◽  
Kevin S. Cannon ◽  
Amy S. Gladfelter
Keyword(s):  
Cell Shape ◽  
Binding Proteins ◽  
Membrane Curvature ◽  
Amphipathic Helix ◽  
Multiple Functions ◽  
Gtp Binding Proteins ◽  
Amphipathic Helices ◽  
Gtp Binding ◽  
Necessary And Sufficient ◽  
Sensing Membrane

AbstractThe curvature of the membrane defines cell shape. Septins are GTP-binding proteins that assemble into heteromeric complexes and polymerize into filaments at areas of micron-scale membrane curvature. An amphipathic helix (AH) domain within the septin complex is necessary and sufficient for septins to preferentially assemble onto micron-scale curvature. Here we report that the non-essential fungal septin, Shs1, also has an AH domain capable of recognizing membrane curvature. In mutants lacking a fully functional Cdc12 AH domain, the Shs1 AH domain becomes essential. Moreover, we find that the Cdc12 AH domain is also important for septin bundling, suggesting multiple functions for septin AH domains.

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