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Plant Physiology Apr 2020Plasma membranes provide a highly selective environment for a large number of transmembrane and membrane-associated proteins. Whereas lateral movement of proteins in... (Review)
Review
Plasma membranes provide a highly selective environment for a large number of transmembrane and membrane-associated proteins. Whereas lateral movement of proteins in this lipid bilayer is possible, it is rather limited in turgid and cell wall-shielded plant cells. However, membrane-resident signaling processes occur on subsecond scales that cannot be explained by simple diffusion models. Accordingly, several receptors and other membrane-associated proteins are organized and functional in membrane nanodomains. Although the general presence of membrane nanodomains has become widely accepted as fact, fundamental functional aspects, the roles of individual lipid species and their interplay with proteins, and aspects of nanodomain maintenance and persistence remain poorly understood. Here, we review the current knowledge of nanodomain organization and function, with a particular focus on signaling processes involving proteins, lipids, and their interactions. Furthermore, we propose new and hypothetical aspects of plant membrane biology that we consider important for future research.
Topics: Cell Membrane; Membrane Microdomains; Models, Biological; Proteolipids; Signal Transduction
PubMed: 31857424
DOI: 10.1104/pp.19.01349 -
Cancer Metastasis Reviews Sep 2018The cell plasma membrane serves as a nexus integrating extra- and intracellular components, which together enable many of the fundamental cellular signaling processes... (Review)
Review
The cell plasma membrane serves as a nexus integrating extra- and intracellular components, which together enable many of the fundamental cellular signaling processes that sustain life. In order to perform this key function, plasma membrane components assemble into well-defined domains exhibiting distinct biochemical and biophysical properties that modulate various signaling events. Dysregulation of these highly dynamic membrane domains can promote oncogenic signaling. Recently, it has been demonstrated that select membrane-targeted dietary bioactives (MTDBs) have the ability to remodel plasma membrane domains and subsequently reduce cancer risk. In this review, we focus on the importance of plasma membrane domain structural and signaling functionalities as well as how loss of membrane homeostasis can drive aberrant signaling. Additionally, we discuss the intricacies associated with the investigation of these membrane domain features and their associations with cancer biology. Lastly, we describe the current literature focusing on MTDBs, including mechanisms of chemoprevention and therapeutics in order to establish a functional link between these membrane-altering biomolecules, tuning of plasma membrane hierarchal organization, and their implications in cancer prevention.
Topics: Animals; Antineoplastic Agents; Biochemical Phenomena; Biomarkers; Biophysical Phenomena; Cell Membrane; Chemoprevention; Dietary Supplements; Humans; Lipid Metabolism; Membrane Lipids; Membrane Microdomains; Membrane Proteins; Neoplasms; Signal Transduction
PubMed: 29860560
DOI: 10.1007/s10555-018-9733-1 -
Current Opinion in Cell Biology Aug 2017The plasma membrane is the most basic element necessary for the cell to exist and be distinguishable from its environment. Regulated mechanisms allow tightly controlled... (Review)
Review
The plasma membrane is the most basic element necessary for the cell to exist and be distinguishable from its environment. Regulated mechanisms allow tightly controlled communication between intacellular and extracellular medium allowing the maintenance of a specific biochemical environment, optimized for cellular functions. The anarchic and uncontrolled opening of a hole in the PM induces a change in the concentration of ions and oxidizing agents perturbing homeostasis. Fortunately, the cell possesses mechanisms that are capable of reacting to sudden extracellular medium entry and to block the leakage locally. Here we summarize the known mechanisms of membrane repair and how the size of the wound and the resulting calcium entry activates preferentially one or another mechanism adapted to the magnitude of the injury.
Topics: Animals; Annexins; Calcium; Cell Membrane; Cell Physiological Phenomena; Cell Survival; Exocytosis; Humans; Lysosomes
PubMed: 28511145
DOI: 10.1016/j.ceb.2017.03.011 -
Nature Chemical Biology Jun 2023Plasma membrane heterogeneity has been tied to a litany of cellular functions and is often explained by analogy to membrane phase separation; however, models based on...
Plasma membrane heterogeneity has been tied to a litany of cellular functions and is often explained by analogy to membrane phase separation; however, models based on phase separation alone fall short of describing the rich organization available within cell membranes. Here we present comprehensive experimental evidence motivating an updated model of plasma membrane heterogeneity in which membrane domains assemble in response to protein scaffolds. Quantitative super-resolution nanoscopy measurements in live B lymphocytes detect membrane domains that emerge upon clustering B cell receptors (BCRs). These domains enrich and retain membrane proteins based on their preference for the liquid-ordered phase. Unlike phase-separated membranes that consist of binary phases with defined compositions, membrane composition at BCR clusters is modulated through the protein constituents in clusters and the composition of the membrane overall. This tunable domain structure is detected through the variable sorting of membrane probes and impacts the magnitude of BCR activation.
Topics: Cell Membrane; Membrane Proteins; Membrane Microdomains
PubMed: 36997644
DOI: 10.1038/s41589-023-01268-8 -
Current Opinion in Cell Biology Feb 2021An intimate interplay of the plasma membrane with curvature-sensing and curvature-inducing proteins would allow for defining specific sites or nanodomains of action at... (Review)
Review
An intimate interplay of the plasma membrane with curvature-sensing and curvature-inducing proteins would allow for defining specific sites or nanodomains of action at the plasma membrane, for example, for protrusion, invagination, and polarization. In addition, such connections are predestined to ensure spatial and temporal order and sequences. The combined forces of membrane shapers and the cortical actin cytoskeleton might hereby in particular be required to overcome the strong resistance against membrane rearrangements in case of high plasma membrane tension or cellular turgor. Interestingly, also the opposite might be necessary, the inhibition of both membrane shapers and cytoskeletal reinforcement structures to relieve membrane tension to protect cells from membrane damage and rupturing during mechanical stress. In this review article, we discuss recent conceptual advances enlightening the interplay of plasma membrane curvature and the cortical actin cytoskeleton during endocytosis, modulations of membrane tensions, and the shaping of entire cells.
Topics: Actin Cytoskeleton; Actins; Animals; Cell Membrane; Cell Shape; Cytoskeleton; Endocytosis; Humans; Yeasts
PubMed: 32927373
DOI: 10.1016/j.ceb.2020.08.008 -
Methods in Molecular Biology (Clifton,... 2023Plasma membrane injury activates membrane trafficking and remodeling events that are required for the injured membrane to repair. With the rapidity of the membrane...
Plasma membrane injury activates membrane trafficking and remodeling events that are required for the injured membrane to repair. With the rapidity of the membrane repair process, the repair response needs to be monitored at high temporal and spatial resolution. In this chapter, we describe the use of live cell optical imaging approaches to monitor injury-triggered bulk and individual vesicle endocytosis. Use of these approaches allows quantitatively assessment of the rate of retrieval of the injured plasma membrane by bulk endocytosis as well as by endocytosis of individual caveolae following plasma membrane injury.
Topics: Endocytosis; Cell Membrane; Synaptic Vesicles
PubMed: 36401047
DOI: 10.1007/978-1-0716-2772-3_27 -
Current Topics in Membranes 2015The organization of eukaryotic membranes into functional domains continues to fascinate and puzzle cell biologists and biophysicists. The lipid raft hypothesis proposes... (Review)
Review
The organization of eukaryotic membranes into functional domains continues to fascinate and puzzle cell biologists and biophysicists. The lipid raft hypothesis proposes that collective lipid interactions compartmentalize the membrane into coexisting liquid domains that are central to membrane physiology. This hypothesis has proven controversial because such structures cannot be directly visualized in live cells by light microscopy. The recent observations of liquid-liquid phase separation in biological membranes are an important validation of the raft hypothesis and enable application of the experimental toolbox of membrane physics to a biologically complex phase-separated membrane. This review addresses the role of giant plasma membrane vesicles (GPMVs) in refining the raft hypothesis and expands on the application of GPMVs as an experimental model to answer some of key outstanding problems in membrane biology.
Topics: Animals; Cell Membrane; Cytoplasmic Vesicles; Humans; Membrane Microdomains; Membranes; Models, Biological
PubMed: 26015280
DOI: 10.1016/bs.ctm.2015.03.009 -
BioEssays : News and Reviews in... Feb 2016The fundamental mechanisms of protein and lipid organization at the plasma membrane have continued to engage researchers for decades. Among proposed models, one idea has... (Review)
Review
The fundamental mechanisms of protein and lipid organization at the plasma membrane have continued to engage researchers for decades. Among proposed models, one idea has been particularly successful which assumes that sterol-dependent nanoscopic phases of different lipid chain order compartmentalize proteins, thereby modulating protein functionality. This model of membrane rafts has sustainably sparked the fields of membrane biophysics and biology, and shifted membrane lipids into the spotlight of research; by now, rafts have become an integral part of our terminology to describe a variety of cell biological processes. But is the evidence clear enough to continue supporting a theoretical concept which has resisted direct proof by observation for nearly twenty years? In this essay, we revisit findings that gave rise to and substantiated the raft hypothesis, discuss its impact on recent studies, and present alternative mechanisms to account for plasma membrane heterogeneity.
Topics: Cell Membrane; Membrane Lipids; Membrane Proteins
PubMed: 26666984
DOI: 10.1002/bies.201500150 -
BioEssays : News and Reviews in... Dec 2023
Topics: Cell Membrane; Lipid Bilayers; Signal Transduction
PubMed: 37840356
DOI: 10.1002/bies.202300191 -
Methods in Molecular Biology (Clifton,... 2021Ras proteins are non-integral membrane proteins, which bind to the plasma membrane by virtue of farnesylation and palmitoylation or a positively charged polybasic...
Ras proteins are non-integral membrane proteins, which bind to the plasma membrane by virtue of farnesylation and palmitoylation or a positively charged polybasic cluster at their C-terminus. Their membrane interactions and/or localization to membrane microdomains, which play important roles in signaling, are regulated by their lateral diffusion at the plasma membrane and their ability to exchange between the membrane and the cytoplasm (binding/unbinding kinetics). Here, using N-Ras as an example, we describe the use of variations of fluorescence recovery after photobleaching (FRAP) to measure the dynamics of the association of N-Ras with the plasma membrane of living cells and their dependence on several parameters (cholesterol, clustering of raft proteins, and palmitoylation/depalmitoylation).
Topics: Cell Membrane; Cytoplasm; Diffusion; Fluorescence Recovery After Photobleaching; Green Fluorescent Proteins; Humans; Membrane Microdomains; Protein Transport; Signal Transduction; ras Proteins
PubMed: 33977477
DOI: 10.1007/978-1-0716-1190-6_10