scholarly journals Loss of hydroxyl groups from the ceramide moiety can modify the lateral diffusion of membrane proteins inS. cerevisiae

2014 ◽  
Vol 55 (7) ◽  
pp. 1343-1356 ◽  
Author(s):  
Satoshi Uemura ◽  
Fumi Shishido ◽  
Motohiro Tani ◽  
Takahiro Mochizuki ◽  
Fumiyoshi Abe ◽  
...  
Keyword(s):  
Membrane Proteins ◽  
Lateral Diffusion ◽  
Hydroxyl Groups ◽  
Ceramide Moiety

scholarly journals Cyclodextrins but not Compactin Inhibit the Lateral Diffusion of Membrane Proteins Independent of Cholesterol

Traffic ◽  
2006 ◽  
Vol 7 (7) ◽  
pp. 917-926 ◽  
Author(s):  
Dmitry E. Shvartsman ◽  
Orit Gutman ◽  
Aliza Tietz ◽  
Yoav I. Henis
Keyword(s):  
Membrane Proteins ◽  
Lateral Diffusion

scholarly journals Periprotein lipidomes of Saccharomyces cerevisiae provide a flexible environment for conformational changes of membrane proteins

eLife ◽  
2020 ◽  
Vol 9 ◽  
Author(s):  
Joury S van 't Klooster ◽  
Tan-Yun Cheng ◽  
Hendrik R Sikkema ◽  
Aike Jeucken ◽  
Branch Moody ◽  
...  
Keyword(s):  
Plasma Membrane ◽  
Membrane Proteins ◽  
Small Molecules ◽  
Conformational Changes ◽  
Direct Detection ◽  
Protein Complexes ◽  
Lateral Diffusion ◽  
Low Ph ◽  
Lipid Particles ◽  
High Degree

Yeast tolerates a low pH and high solvent concentrations. The permeability of the plasma membrane (PM) for small molecules is low and lateral diffusion of proteins is slow. These findings suggest a high degree of lipid order, which raises the question of how membrane proteins function in such an environment. The yeast PM is segregated into the Micro-Compartment-of-Can1 (MCC) and Pma1 (MCP), which have different lipid compositions. We extracted proteins from these microdomains via stoichiometric capture of lipids and proteins in styrene-maleic-acid-lipid-particles (SMALPs). We purified SMALP-lipid-protein complexes by chromatography and quantitatively analyzed periprotein lipids located within the diameter defined by one SMALP. Phospholipid and sterol concentrations are similar for MCC and MCP, but sphingolipids are enriched in MCP. Ergosterol is depleted from this periprotein lipidome, whereas phosphatidylserine is enriched relative to the bulk of the plasma membrane. Direct detection of PM lipids in the 'periprotein space' supports the conclusion that proteins function in the presence of a locally disordered lipid state.

Lipid fluidity and membrane protein dynamics

1987 ◽  
Vol 7 (11) ◽  
pp. 823-837 ◽  
Author(s):  
Giorgio Lenaz
Keyword(s):  
Electron Transfer ◽  
Catalytic Activity ◽  
Membrane Proteins ◽  
Conformational Changes ◽  
Inner Core ◽  
Lateral Diffusion ◽  
Protein Molecule ◽  
Thermal Fluctuations ◽  
Membrane Diffusion ◽  
Lipid Fluidity

Membrane fluidity plays an important role in cellular functions. Membrane proteins are mobile in the lipid fluid environment; lateral diffusion of membrane proteins is slower than expected by theory, due to both the effect of protein crowding in the membrane and to constraints from the aqueous matrix. A major aspect of diffusion is in macromolecular associations: reduction of dimensionality for membrane diffusion facilitates collisional encounters, as those concerned with receptor-mediated signal transduction and with electron transfer chains. In mitochondrial electron transfer, diffusional control is prevented by the excess of collisional encounters between fast-diffusing ubiquinone and the respiratory complexes. Another aspect of dynamics of membrane proteins is their conformational flexibility. Lipids may induce the optimal conformation for catalytic activity. Breaks in Arrhenius plots of membrane-bound enzymes may be related to lipid fluidity: the break could occur when a limiting viscosity is reached for catalytic activity. Viscosity can affect protein conformational changes by inhibiting thermal fluctuations to the inner core of the protein molecule.

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