Influence of proteins on the reorganization of phospholipid bilayers into large domains

Haverstick, Doris M.; Gläser, Michael

doi:10.1016/s0006-3495(89)82866-8

Cited by 62 publications

(33 citation statements)

References 36 publications

(33 reference statements)

Supporting

Mentioning

Contrasting

Order By: Relevance

“…These results are consistent with the observations of Kimelberg et al, 31 who suggested an electrostatic mechanism for cytochrome c adsorption to the membrane. Domain formation of cytochrome c adsorbing to acidic lipid bilayers has already been observed by Haverstick and Glaser 56 at low salt concentrations using fluorescence/optical microscopy on vesicle suspensions. These authors reported aggregation of the negatively charged lipids in those regions where cytochrome c had adsorbed.…”

Section: Resultssupporting

confidence: 57%

Adsorption of Membrane-Associated Proteins to Lipid Bilayers Studied with an Atomic Force Microscope: Myelin Basic Protein and Cytochrome c

2000

View full text Add to dashboard Cite

Atomic force microscopy was used to study the structure of two membrane-associated proteins adsorbed to various supported phospholipid bilayers in physiological buffer. The aim was (a) to develop a preparation for the investigation of membrane-associated proteins at high resolution under native conditions and (b) to obtain information about the factors that determine the adsorption process and the structure of adsorbed proteins. Therefore, solid-supported membranes were formed on mica by spontaneous vesicle adsorption and spreading. Once a homogeneous, pinhole-free bilayer was formed, solutions containing the proteins at appropriate concentrations were applied. The two positively charged proteins chosen were myelin basic protein (MBP), which plays an essential role in the formation of functional myelin, and cytochrome c. On charged bilayers, MBP applied at concentrations of 0.5-50 µg/mL formed aggregates of defined height (1.9 ( 0.2 nm on negatively and 2.7 ( 0.2 nm on positively charged lipids), which at high concentration covered the entire bilayer. These aggregates are probably monomolecular layers of MBP. On neutral lipid adsorbed MBP formed irregular aggregates. Cytochrome c showed a different adsorption: On negatively charged lipid it formed aggregates of defined, monomolecular height (3.3 ( 0.2 nm). On neutral bilayers small aggregates were observed. On positively charged lipid no adsorption was observed at all. These results indicate that (a) the adsorption of cytomchrome c can be interpreted in terms of a dominating electrostatic interaction; (b) MBP adsorption to lipid bilayers is not exclusively electrostatically driven and depends on the specific lipid bilayer composition; (c) the structure of adsorbed aggregates indicates a strong protein-protein interaction.

show abstract

Section: Resultssupporting

confidence: 57%

Adsorption of Membrane-Associated Proteins to Lipid Bilayers Studied with an Atomic Force Microscope: Myelin Basic Protein and Cytochrome c

2000

View full text Add to dashboard Cite

show abstract

“…The increased size and enrichment of the lipid domains in membranes after protein aggregation is consistent with the role of the proteins in forming the domains. It has been shown that some proteins can cause nonrandom distributions of lipids in a bilayer (15,55). It is possible that certain proteins in the erythrocyte membrane are not uniformly distributed, perhaps through interactions with the cytoskeleton, and that the proteins induce the formation of the lipid domains.…”

Section: Discussionmentioning

confidence: 99%

“…A similar phenomenon occurs when cytochrome c, or other basic proteins, bind to membranes containing acidic phospholipids (15)(16)(17)(18)(19)(20)(21)(22).…”

mentioning

confidence: 90%

“…Lipids in domains of nonbilayer phases also have been postulated to occur in biological membranes (46), and additional evidence is needed to determine how extensive these phases are under physiological conditions. Direct visualization of membrane domains using fluorescence digital imaging microscopy offers the best means for demonstrating their existence (7,15,50). This paper reports studies using this method to collect and analyze images of fluorescently labeled erythrocyte membranes.…”

mentioning

confidence: 99%

See 1 more Smart Citation

Characterization of lipid domains in erythrocyte membranes.

Rodgers

Gläser

1991

Proc. Natl. Acad. Sci. U.S.A.

View full text Add to dashboard Cite

Fluorescence digital imaging microscopy was used to study the lateral distribution of the lipid components in erythrocyte membranes. Intact erythrocytes labeled with phospholipids containing a fluorophore attached to one fatty acid chain showed an uneven distribution ofthe phospholipids in the membrane thereby demonstrating the presence of membrane domains. The enrichment of the lipotropic compound chlorpromazine in domains in intact erythrocytes also suggested that the domains are lipid-enriched regions. Similar membrane domains were present in erythrocyte ghosts. The phospholipid enrichment was increased in the domains by inducing membrane protein aggregation. Double-labeling experiments were done to determine the relative distributions of different phospholipids in the membrane. Vesicles made from extracted lipids did not show the presence of domains consistent with the conclusion that membrane proteins were responsible for creating the domains. Overall, it was found that large domains exist in the red blood cell membrane with unequal enrichment of the different phospholipid species.Since it was proposed almost 20 years ago, the Fluid Mosaic Model has served as a foundation for understanding membrane structure and function (1). The model describes biological membranes as a mixture of lipid and protein components in a phospholipid bilayer where all the components can undergo free lateral motion. This results in a random distribution of the membrane components with no long-range order. One refinement to this model is the role of the cytoskeleton in anchoring transmembrane proteins (2). Another change is that biological membranes may be more heterogeneous than depicted by the Fluid Mosaic Model with the existence of relatively large domains with compositions different from the bulk membrane.

show abstract

“…24 In addition, Glaser and co-workers also studied lipid domain formation induced by addition of proteins and peptides in GUV membranes. [33][34][35] In addition to their use in membrane research, GUVs have been used as membrane models in a number of studies of lipid-protein and lipid-DNA interactions. 36-4° In these reports, a novel approach was taken, consisting of depositing femtoliter amounts of DNA or protein solutions onto GUVs and then monitoring the subsequent binding events and vesicle morphology changes by optical microscopy (phase contrast or epifluorescence).…”

Section: Microscopy Techniques and Giant Unilamellar Vesiclesmentioning

confidence: 99%

[20] Giant vesicles, laurdan, and two-photon fluorescence microscopy: Evidence of lipid lateral separation in bilayers

Bagatolli¹,

Sánchez²,

Hazlett³

et al. 2003

Methods in Enzymology

102

View full text Add to dashboard Cite

Influence of proteins on the reorganization of phospholipid bilayers into large domains

Cited by 62 publications

References 36 publications

Adsorption of Membrane-Associated Proteins to Lipid Bilayers Studied with an Atomic Force Microscope: Myelin Basic Protein and Cytochrome c

Adsorption of Membrane-Associated Proteins to Lipid Bilayers Studied with an Atomic Force Microscope: Myelin Basic Protein and Cytochrome c

Characterization of lipid domains in erythrocyte membranes.

[20] Giant vesicles, laurdan, and two-photon fluorescence microscopy: Evidence of lipid lateral separation in bilayers

Contact Info

Product

Resources

About