Steric Pressure between Membrane-Bound Proteins Opposes Lipid Phase Separation

2013 ◽  
Vol 135 (4) ◽  
pp. 1185-1188 ◽  
Author(s):  
Christine S. Scheve ◽  
Paul A. Gonzales ◽  
Noor Momin ◽  
Jeanne C. Stachowiak
Keyword(s):  
Phase Separation ◽  
Lipid Phase ◽  
Membrane Bound ◽  
Lipid Phase Separation

scholarly journals Glucagon-stimulated adenylate cyclase detects a selective perturbation of the inner half of the liver plasma-membrane bilayer achieved by the local anaesthetic prilocaine

1980 ◽  
Vol 190 (1) ◽  
pp. 131-137 ◽  
Author(s):  
M D Houslay ◽  
I Dipple ◽  
S Rawal ◽  
R D Sauerheber ◽  
J A Esgate ◽  
...  
Keyword(s):  
Phase Separation ◽  
Fatty Acid ◽  
Adenylate Cyclase ◽  
Rat Liver ◽  
Spin Probe ◽  
Plasma Membranes ◽  
Lipid Phase ◽  
Rat Liver Plasma Membranes ◽  
Membrane Bound ◽  
Lipid Phase Separation

Prilocaine can increase the fluidity of rat liver plasma membranes, as indicated by a fatty acid spin-probe. This led to the activation of the membrane-bound fluoride-stimulated adenylate cyclase activity, but not the Lubrol-solubilized activity, suggesting that increased lipid fluidity can activate the enzyme. With increasing prilocaine concentrations above 10 mM, the membrane-bound fluoride-stimulated activity was progressively inhibited, even though bilayer fluidity continued to increase and the activity of the solubilized enzyme remained unaffected. Glucagon-stimulated adenylate cyclase was progressively inhibited by increasing prilocaine concentrations. Prilocaine (10 mM) had no effect on the lipid phase separation occurring at 28 degrees C and attributed to those lipids in the external half of the bilayer, as indicated by Arrhenius plots of both glucagon-stimulated adenylate cyclase activity and the order parameter of a fatty acid spin-probe. However, 10 mM-prilocaine induced a lipid phase separation at around 11 degrees C that was attributed to the lipids of the internal (cytosol-facing) half of the bilayer. It is suggested that prilocaine (10 mM) can selectively perturb the inner half of the bilayer of rat liver plasma membranes owing to its preferential interaction with the acidic phospholipids residing there.

scholarly journals Steric Pressure among Membrane-Bound Polymers Opposes Lipid Phase Separation

2016 ◽  
Vol 110 (3) ◽  
pp. 70a-71a
Author(s):  
Zachary I. Imam ◽  
Laura Kenyon ◽  
Jeanne Stachowiak
Keyword(s):  
Phase Separation ◽  
Lipid Phase ◽  
Membrane Bound ◽  
Lipid Phase Separation

scholarly journals Steric Pressure among Membrane-Bound Polymers Opposes Lipid Phase Separation

Langmuir ◽  
2016 ◽  
Vol 32 (15) ◽  
pp. 3774-3784 ◽  
Author(s):  
Zachary I. Imam ◽  
Laura E. Kenyon ◽  
Adelita Carrillo ◽  
Isai Espinoza ◽  
Fatema Nagib ◽  
...  
Keyword(s):  
Phase Separation ◽  
Lipid Phase ◽  
Membrane Bound ◽  
Lipid Phase Separation

Intermolecular hydrogen bonding between lipids: influence on organization and function of lipids in membranes

1980 ◽  
Vol 58 (10) ◽  
pp. 755-770 ◽  
Author(s):  
Joan M. Boggs
Keyword(s):  
Hydrogen Bonding ◽  
Phase Separation ◽  
Dynamic Equilibrium ◽  
Hexagonal Phase ◽  
Intermolecular Forces ◽  
Lipid Phase ◽  
Intermolecular Hydrogen Bonding ◽  
Extracellular Stimuli ◽  
And Function ◽  
Lipid Phase Separation

Biological membranes have unique lipid compositions suggesting a specific role for many lipids. Evidence is reviewed concerning the intermolecular forces between glycero- and sphingolipids and cholesterol, the dependence of many of these interactions on the state of ionization of lipids, pH, ionic strength, and divalent cation concentration. The effect of intermolecular interactions between certain lipids on lipid clustering, interaction with cholesterol, on the conformation of proteins, and on transitions to the hexagonal phase is considered. Other forces which cause lipid phase separation or clustering are discussed. It is concluded that lipids are in dynamic equilibrium with their environment and can act as receptors for certain intra- or extracellular stimuli, which they can translate into a response by undergoing changes in fluidity, phase transitions, or phase separation.

Lipid phase separation induced by a hydrophobic protein in phosphatidylserine-phosphatidylcholine vesicles

Biochemistry ◽  
1977 ◽  
Vol 16 (11) ◽  
pp. 2325-2329 ◽  
Author(s):  
J. M. Boggs ◽  
D. D. Wood ◽  
M. A. Moscarello ◽  
D. Papahadjopoulos
Keyword(s):  
Phase Separation ◽  
Lipid Phase ◽  
Hydrophobic Protein ◽  
Lipid Phase Separation

scholarly journals Coupling between lipid miscibility and phosphotyrosine driven protein condensation at the membrane

2020 ◽  
Author(s):  
J. K. Chung ◽  
W. Y. C. Huang ◽  
C. B. Carbone ◽  
L. M. Nocka ◽  
A. N. Parikh ◽  
...  
Keyword(s):  
Phase Transition ◽  
Phase Transitions ◽  
Phase Separation ◽  
Membrane Surface ◽  
Adaptor Protein ◽  
Receptor Activation ◽  
Lipid Phase ◽  
Two Dimensional ◽  
Sos Protein ◽  
Lipid Phase Separation

AbstractLipid miscibility phase separation has long been considered to be a central element of cell membrane organization. More recently, protein condensation phase transitions, into three-dimensional droplets or in two-dimensional lattices on membrane surfaces, have emerged as another important organizational principle within cells. Here, we reconstitute the LAT:Grb2:SOS protein condensation on the surface of giant unilamellar vesicles capable of undergoing lipid phase separations. Our results indicate that assembly of the protein condensate on the membrane surface can drive lipid phase separation. This phase transition occurs isothermally and is governed by tyrosine phosphorylation on LAT. Furthermore, we observe that the induced lipid phase separation drives localization of the SOS substrate, K-Ras, into the LAT:Grb2:SOS protein condensate.Statement of SignificanceProtein condensation phase transitions are emerging as an important organizing principles in cells. One such condensate plays a key role in T cell receptor signaling. Immediately after receptor activation, multivalent phosphorylation of the adaptor protein LAT at the plasma membrane leads to networked assembly of a number of signaling proteins into a two-dimensional condensate on the membrane surface. In this study, we demonstrate that LAT condensates in reconstituted vesicles are sufficient to drive lipid phase separation. This lipid reorganization drives another key downstream signaling molecule, Ras, into the LAT condensates. These results show that the LAT condensation phase transition, which is actively controlled by phosphorylation reactions, extends its influence to control lipid phase separation in the underlying membrane.

scholarly journals Gangliosides Destabilize Lipid Phase Separation in Multicomponent Membranes

2019 ◽  
Vol 117 (7) ◽  
pp. 1215-1223 ◽  
Author(s):  
Yang Liu ◽  
Jonathan Barnoud ◽  
Siewert J. Marrink
Keyword(s):  
Phase Separation ◽  
Lipid Phase ◽  
Lipid Phase Separation
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