Regulation of membrane lipid bilayer structure during salinity adaptation: A study with the gill epithelial cell membranes of Oreochromis niloticus

2005 ◽  
Vol 142 (1) ◽  
pp. 28-36 ◽  
Author(s):  
P. Shivkamat ◽  
R. Roy
Keyword(s):  
Epithelial Cell ◽  
Lipid Bilayer ◽  
Oreochromis Niloticus ◽  
Cell Membranes ◽  
Membrane Lipid ◽  
Bilayer Structure ◽  
Salinity Adaptation ◽  
Membrane Lipid Bilayer

scholarly journals The modulation of protein kinase C activity by membrane lipid bilayer structure.

1994 ◽  
Vol 269 (7) ◽  
pp. 4866-4871 ◽  
Author(s):  
S.J. Slater ◽  
M.B. Kelly ◽  
F.J. Taddeo ◽  
C. Ho ◽  
E. Rubin ◽  
...  
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Lipid Bilayer ◽  
Membrane Lipid ◽  
Bilayer Structure ◽  
Kinase C ◽  
Protein Kinase C Activity ◽  
Membrane Lipid Bilayer

scholarly journals PHLIP ARG-Mutant Interactions with the Membrane Lipid Bilayer

2021 ◽  
Vol 120 (3) ◽  
pp. 232a
Author(s):  
Hannah M. Visca ◽  
Oleg A. Andreev ◽  
Yana K. Reshetnyak
Keyword(s):  
Lipid Bilayer ◽  
Membrane Lipid ◽  
Membrane Lipid Bilayer

The Power of Asymmetry: Architecture and Assembly of the Gram-Negative Outer Membrane Lipid Bilayer

2016 ◽  
Vol 70 (1) ◽  
pp. 255-278 ◽  
Author(s):  
Jeremy C. Henderson ◽  
Shawn M. Zimmerman ◽  
Alexander A. Crofts ◽  
Joseph M. Boll ◽  
Lisa G. Kuhns ◽  
...  
Keyword(s):  
Outer Membrane ◽  
Lipid Bilayer ◽  
Membrane Lipid ◽  
Gram Negative ◽  
Membrane Lipid Bilayer

scholarly journals Anomalous behavior of water inside the SecY translocon

2015 ◽  
Vol 112 (29) ◽  
pp. 9016-9021 ◽  
Author(s):  
Sara Capponi ◽  
Matthias Heyden ◽  
Ana-Nicoleta Bondar ◽  
Douglas J. Tobias ◽  
Stephen H. White
Keyword(s):  
Membrane Proteins ◽  
Lipid Bilayer ◽  
Pyrococcus Furiosus ◽  
Hydrophobic Effect ◽  
Accessible Surface Area ◽  
Anomalous Behavior ◽  
Membrane Lipid ◽  
Nascent Chain ◽  
Membrane Lipid Bilayer ◽  
Dynamics Simulations

The heterotrimeric SecY translocon complex is required for the cotranslational assembly of membrane proteins in bacteria and archaea. The insertion of transmembrane (TM) segments during nascent-chain passage through the translocon is generally viewed as a simple partitioning process between the water-filled translocon and membrane lipid bilayer, suggesting that partitioning is driven by the hydrophobic effect. Indeed, the apparent free energy of partitioning of unnatural aliphatic amino acids on TM segments is proportional to accessible surface area, which is a hallmark of the hydrophobic effect [Öjemalm K, et al. (2011) Proc Natl Acad Sci USA 108(31):E359–E364]. However, the apparent partitioning solvation parameter is less than one-half the value expected for simple bulk partitioning, suggesting that the water in the translocon departs from bulk behavior. To examine the state of water in a SecY translocon complex embedded in a lipid bilayer, we carried out all-atom molecular-dynamics simulations of the Pyrococcus furiosus SecYE, which was determined to be in a “primed” open state [Egea PF, Stroud RM (2010) Proc Natl Acad Sci USA 107(40):17182–17187]. Remarkably, SecYE remained in this state throughout our 450-ns simulation. Water molecules within SecY exhibited anomalous diffusion, had highly retarded rotational dynamics, and aligned their dipoles along the SecY transmembrane axis. The translocon is therefore not a simple water-filled pore, which raises the question of how anomalous water behavior affects the mechanism of translocon function and, more generally, the partitioning of hydrophobic molecules. Because large water-filled cavities are found in many membrane proteins, our findings may have broader implications.

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