scholarly journals Phosphatidylserine prevents the generation of a protein-free giant plasma membrane domain in yeast

2020 ◽  
Author(s):  
Tetsuo Mioka ◽  
Guo Tian ◽  
Wang Shiyao ◽  
Takuma Tsuji ◽  
Takuma Kishimoto ◽  
...  
Keyword(s):  
Plasma Membrane ◽  
Phase Separation ◽  
Living Cells ◽  
Yeast Cells ◽  
Membrane Domains ◽  
Membrane Domain ◽  
Artificial Membranes ◽  
Free Region ◽  
Large Phase ◽  
Plasma Membrane Domains

AbstractMembrane phase separation accompanied with micron-scale domains of lipids and proteins occurs in artificial membranes; however, a similar large phase separation has not been reported in the plasma membrane of the living cells. We demonstrate here that a stable micron-scale protein-free region is generated in the plasma membrane of the yeast mutants lacking phosphatidylserine. We named this region the “void zone”. Transmembrane proteins, peripheral membrane proteins, and certain phospholipids are excluded from the void zone. The void zone is rich in ergosterol and requires ergosterol and sphingolipids for its formation. These characteristics of the void zone are similar to the properties of the cholesterol-enriched domain in phase-separated artificial membranes. We propose that phosphatidylserine prevents the formation of the void zone by preferentially interacting with ergosterol. We also found that void zones were frequently in contact with vacuoles, in which a membrane domain was also formed at the contact site.Summary statementYeast cells lacking phosphatidylserine generate protein-free plasma membrane domains, and vacuoles contact with this domain. This is the first report of micron-scale plasma membrane domains in living cells.

scholarly journals Characterization of micron-scale protein-depleted plasma membrane domains in phosphatidylserine-deficient yeast cells

2021 ◽  
Vol 135 (5) ◽  
Author(s):  
Tetsuo Mioka ◽  
Tian Guo ◽  
Shiyao Wang ◽  
Takuma Tsuji ◽  
Takuma Kishimoto ◽  
...  
Keyword(s):  
Plasma Membrane ◽  
Phase Separation ◽  
Large Scale ◽  
Living Cells ◽  
Yeast Cells ◽  
Membrane Domain ◽  
Cellular Functions ◽  
Artificial Membranes ◽  
Yeast Mutants

ABSTRACT Membrane phase separation to form micron-scale domains of lipids and proteins occurs in artificial membranes; however, a similar large-scale phase separation has not been reported in the plasma membrane of the living cells. We show here that a stable micron-scale protein-depleted region is generated in the plasma membrane of yeast mutants lacking phosphatidylserine at high temperatures. We named this region the ‘void zone’. Transmembrane proteins and certain peripheral membrane proteins and phospholipids are excluded from the void zone. The void zone is rich in ergosterol, and requires ergosterol and sphingolipids for its formation. Such properties are also found in the cholesterol-enriched domains of phase-separated artificial membranes, but the void zone is a novel membrane domain that requires energy and various cellular functions for its formation. The formation of the void zone indicates that the plasma membrane in living cells has the potential to undergo phase separation with certain lipid compositions. We also found that void zones were frequently in contact with vacuoles, in which a membrane domain was also formed at the contact site.

scholarly journals Rapid Nonvesicular Transport of Sterol between the Plasma Membrane Domains of Polarized Hepatic Cells

2002 ◽  
Vol 277 (33) ◽  
pp. 30325-30336
Author(s):  
Daniel Wüstner ◽  
Andreas Herrmann ◽  
Mingming Hao ◽  
Frederick R. Maxfield
Keyword(s):  
Plasma Membrane ◽  
Membrane Domains ◽  
Hepatic Cells ◽  
Plasma Membrane Domains

scholarly journals Stabilizing membrane domains antagonizes n-alcohol anesthesia

2016 ◽  
Author(s):  
B.B. Machta ◽  
E. Grey ◽  
M. Nouri ◽  
N.L.C. McCarthy ◽  
E.M. Gray ◽  
...  
Keyword(s):  
Plasma Membrane ◽  
Phase Separation ◽  
Critical Temperature ◽  
Hydrostatic Pressure ◽  
General Anesthesia ◽  
Membrane Domains ◽  
Strongly Correlated ◽  
Membrane Heterogeneity ◽  
Anesthetic Potency ◽  
Better Than

AbstractDiverse molecules induce general anesthesia with potency strongly correlated both with their hydrophobicity and their effects on certain ion channels. We recently observed that several n-alcohol anesthetics inhibit heterogeneity in plasma membrane derived vesicles by lowering the critical temperature (Tc) for phase separation. Here we exploit conditions that stabilize membrane heterogeneity to further test the correlation between the anesthetic potency of n-alcohols and effects on Tc. First we show that hexadecanol acts oppositely to n-alcohol anesthetics on membrane mixing and antagonizes ethanol induced anesthesia in a tadpole behavioral assay. Second, we show that two previously described ‘intoxication reversers’ raise Tc and counter ethanol’s effects in vesicles, mimicking the findings of previous electrophysiological and behavioral measurements. Third, we find that hydrostatic pressure, long known to reverse anesthesia, also raises Tc in vesicles with a magnitude that counters the effect of butanol at relevant concentrations and pressures. Taken together,these results demonstrate that ΔTc predicts anesthetic potency for n-alcohols better than hydrophobicity in a range of contexts, supporting a mechanistic role for membrane heterogeneity in general anesthesia.

scholarly journals Synergistic Assembly of Linker for Activation of T Cells Signaling Protein Complexes in T Cell Plasma Membrane Domains

2003 ◽  
Vol 278 (22) ◽  
pp. 20389-20394 ◽  
Author(s):  
Lorian C. Hartgroves ◽  
Joseph Lin ◽  
Hanno Langen ◽  
Tobias Zech ◽  
Arthur Weiss ◽  
...  
Keyword(s):  
T Cells ◽  
Plasma Membrane ◽  
T Cell ◽  
Protein Complexes ◽  
Membrane Domains ◽  
Cell Plasma Membrane ◽  
Signaling Protein ◽  
Cell Plasma ◽  
Plasma Membrane Domains

Molecular events in the organization of renal tubular epithelium: from nephrogenesis to regeneration

1989 ◽  
Vol 257 (6) ◽  
pp. F913-F924 ◽  
Author(s):  
R. Bacallao ◽  
L. G. Fine
Keyword(s):  
Plasma Membrane ◽  
Spatial Organization ◽  
Cell Interaction ◽  
Acute Injury ◽  
External Signal ◽  
Renal Tubular Cell ◽  
Membrane Domains ◽  
Sequence Of Events ◽  
Plasma Membrane Domains ◽  
Renal Tubular

Information from studies of embryonic nephrons and established renal tubular cell lines in culture can be integrated to derive a picture of how the renal tubule develops and regenerates after acute injury. During development, the formation of a morphologically polarized epithelium from committed nephric mesenchymal cells requires an external signal for mitogenesis and differentiation. Polypeptide growth factors, in some cases mediated through oncogene expression, act in an autocrine or paracrine fashion to stimulate the production of extracellular matrix proteins that probably provide the earliest orientation signal for the cell. Interaction of these proteins with cell surface receptors leads to early organization of the cytoskeletal actin network, which is the major scaffolding for further differentiation and for definition of plasma membrane domains. The formation of cell-cell contacts via specialized adhesion molecules integrates the epithelium into a polarized monolayer and maintains its fence function, i.e., separation of plasma membrane domains. Microtubules probably participate in the delivery of vesicles to specific plasma membrane domains and in the spatial organization of intracellular organelles. Following acute renal injury, this sequence of events appears to be reversed, resulting in partial or complete loss of differentiated features. Regeneration seems to follow the same pattern of sequential differentiation steps as nephrogenesis. The integrity of the epithelium is restored by reestablishing only those stages of differentiation that have been lost. Where cell death occurs, mitogenesis in adjacent cells restores the continuity of the epithelium and the entire sequence of differentiation events is initiated in the newly generated cells.

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