Lipid domains and lipid/protein interactions in biological membranes

Tocanne, Jean‐François; Cézanne, Laurence; Lopez, André; Piknová, Barbora; Schram, Vincent; Tournier, Jean-François; Welby, Michèle

doi:10.1016/0009-3084(94)90179-1

Cited by 115 publications

(86 citation statements)

References 84 publications

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“…As summarized in Box 1, studies in model systems have shown that in phase-separated bilayers of heterogeneous composition, TMDs partition into the phase that best matches their length. Additionally, in non-phase-separated bilayers of heterogeneous composition, an integrated TMD can trigger lateral segregation of lipids by recruiting those species that are best matched to its length (Sperotto and Mouritsen, 1993;Tocanne et al, 1994;Killian, 1998;Kaiser et al, 2011). Importantly, even in bilayers of homogeneous composition, positively mismatched TMDs locally increase bilayer thickness by stretching the phospholipid fatty acyl chains.…”

Section: Lipid-dependent Sortingmentioning

confidence: 99%

Getting membrane proteins on and off the shuttle bus between the endoplasmic reticulum and the Golgi complex

Borgese

2016

Journal of Cell Science

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Secretory proteins exit the endoplasmic reticulum (ER) in coat protein complex II (COPII)-coated vesicles and then progress through the Golgi complex before delivery to their final destination. Soluble cargo can be recruited to ER exit sites by signal-mediated processes (cargo capture) or by bulk flow. For membrane proteins, a third mechanism, based on the interaction of their transmembrane domain (TMD) with lipid microdomains, must also be considered. In this Commentary, I review evidence in favor of the idea that partitioning of TMDs into bilayer domains that are endowed with distinct physico-chemical properties plays a pivotal role in the transport of membrane proteins within the early secretory pathway. The combination of such selforganizational phenomena with canonical intermolecular interactions is most likely to control the release of membrane proteins from the ER into the secretory pathway.

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Section: Lipid-dependent Sortingmentioning

confidence: 99%

Getting membrane proteins on and off the shuttle bus between the endoplasmic reticulum and the Golgi complex

Borgese

2016

Journal of Cell Science

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“…Recent studies of this mutant have revealed that E. coli synthesizes its membrane lipids, principally cardiolipin, which binds calcium, so as to maintain a particular proportion of its lipids with a propensity to form type II nonbilayer structures in the presence of divalent ions (37). The formation of lateral domains in membranes occurs in both eukaryotic and prokaryotic cells (44,80). A role for calcium is suspected since calcium mediates the formation of lateral domains of acidic phospholipids in vitro and possibly in vivo (reference 53 and references therein).…”

Section: Mechanismsmentioning

confidence: 99%

Calcium signalling in bacteria

et al. 1996

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In eukaryotic cells, variations in the levels of cytosolic free calcium regulate processes as important and disparate as chemotaxis, chromosome segregation, fertilization, ion transport, muscle contraction, passage through cell cycle transition points, proteolysis, secretion, and substrate uptake (7). Cytosolic free calcium concentration is tightly controlled by the action of specific pumps and channels in the plasma membrane and subcellular organelles (8,83). Response to increased cytosolic free calcium concentration is mediated by either direct binding to calcium-sensitive enzymes, such as protein kinase C (49) and calpain (72), or activation of a protein transducer, such as calmodulin (15).In prokaryotic cells, an equivalent important role for calcium has been harder to demonstrate but is now becoming evident (53,59,69). Research on a variety of bacterial processes has passed from the phase of demonstrating a likely involvement of calcium to clarifying the nature of this involvement. In this minireview, recent evidence on the existence of bacterial components (both proteinaceous and nonproteinaceous) concerned with calcium regulation is evaluated, since investigation of these components is one of the surest routes to confirming the involvement of calcium in a process. These components include voltage-gated calcium channels responsible for influx that can be formed from poly-3-hydroxybutyratepolyphosphate complexes, primary and secondary transporters responsible for efflux, and calmodulin-like proteins responsible for mediating responses to calcium. Such calcium-dependent regulation may be exerted directly by changes in nucleoid structure or indirectly by phosphorylation or proteolysis of target proteins. Despite the problems sometimes associated with studies of calcium, this ion is increasingly implicated in a number of bacterial functions, including heat shock, pathogenicity, chemotaxis, differentiation, and the cell cycle. INTRACELLULAR CALCIUM LEVELSEstimates of the intracellular free calcium concentration of 0.1 and 1 M in the model organism Escherichia coli have been obtained with Fura-2 {1-[2-(5-carboxyoxazol-2-yl)-6-aminobenzofuran -5 -oxy] -2-(2Ј -amino -5Ј -methylphenoxy)ethane-N,N,NЈ,NЈ-tetraacetic acid} (24, 77) and aequorin (85), respectively. Such levels are similar to those in eukaryotic cells and are a 1,000 times less than those typically found outside the cell. Three factors are considered responsible for this low level: the low permeability of the envelope with tightly controlled influx mechanisms, a high buffering capacity, and effective export systems. CALCIUM INFLUXIn eukaryotic cells, a number of mechanisms for gated entry of calcium have been characterized. Families of calcium channels have been identified, which can be classified broadly by the stimulus for channel opening into voltage-operated, receptoroperated, mechanically operated or tonically active calcium channels (83). In particular, eukaryotic L-type, voltage-operated calcium channels (VOCCs) are activated by membrane depolari...

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“…The assembly of opposed phospholipid monolayers in a lipid bilayer is considered to be weak, [40] which is in agreement with the fact that phase transitions in liposomes can take place in one leaflet independent of the other. [4, 32-34, 36, 41] Model phospholipid monolayers are a simple, controllable and well-defined system to study interactions in the lipid backbone of biomembranes, as well as other biological reactions in two dimensions.…”

Section: Model Membranesmentioning

confidence: 84%

Electrochemical Properties of Phospholipid Monolayers at Liquid–Liquid Interfaces

Santos¹,

Garcı́a-Morales²,

Pereira³

2010

ChemPhysChem

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Biomembrane models built at the interface between two immiscible electrolytes (ITIES) are useful systems to study phenomena of biological relevance by means of their electrochemical processes. The unique properties of ITIES allow one either to control or measure the potential difference across the biomimetic membranes. Herein we focus on phospholipid monolayers adsorbed at liquid-liquid interfaces, and besides discussing recent developments on the subject, we describe electrochemical techniques that can be used to get insight on the interfacial processes and electrostatic properties of phospholipid membranes at the ITIES. In particular, we examine the electrochemical and physicochemical properties of (modified) phospholipid monolayers and their interaction with other biologically relevant compounds. The use of liquid-liquid electrochemistry as a powerful tool to characterize drug properties is outlined. Although this review is not a survey of all the work in the field, it provides a comprehensive referencing to current research.

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Lipid domains and lipid/protein interactions in biological membranes

Cited by 115 publications

References 84 publications

Getting membrane proteins on and off the shuttle bus between the endoplasmic reticulum and the Golgi complex

Getting membrane proteins on and off the shuttle bus between the endoplasmic reticulum and the Golgi complex

Calcium signalling in bacteria

Electrochemical Properties of Phospholipid Monolayers at Liquid–Liquid Interfaces

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