Phase behavior and the partitioning of caveolin-1 scaffolding domain peptides in model lipid bilayers

Horton, Margaret R.; Rädler, Joachim O.; Gast, Alice P.

doi:10.1016/j.jcis.2006.08.057

Cited by 12 publications

(12 citation statements)

References 56 publications

(70 reference statements)

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“…This observation likely indicates that the concept of caveolae as a liquid-ordered phase contained in a coexisting Ld membrane phase is oversimplified. It seems to be in accordance, however, with studies that have described newly synthesized caveolin in the Golgi apparatus not to be associated with detergent resistant membranes [50] and with a model membrane study that described the caveolin scaffolding domain of caveolin-1 to be Ld phase preferring[51]. …”

Section: Resultssupporting

confidence: 83%

Temperature-dependent phase behavior and protein partitioning in giant plasma membrane vesicles

Johnson

Stinson

et al. 2010

Biochimica et Biophysica Acta (BBA) - Biomembranes

102

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Liquid-ordered (Lo) and liquid-disordered (Ld) phase coexistence has been suggested to partition the plasma membrane of biological cells into lateral compartments, allowing for enrichment or depletion of functionally relevant molecules. This dynamic partitioning might be involved in fine-tuning cellular signaling fidelity through coupling to the plasma membrane protein and lipid composition. In earlier work, giant plasma membrane vesicles, obtained by chemically induced blebbing from cultured cells, were observed to reversibly phase segregate at temperatures significantly below 37 °C. In this contribution, we compare the temperature dependence of fluid phase segregation in HeLa and Rat basophilic leukemia (RBL) cells. We find an essentially monotonic temperature dependence of the number of phase separated vesicles in both cell types. We also observe a strikingly broad distribution of phase transition temperatures in both cell types. The binding of peripheral proteins, such as cholera toxin subunit B (CTB), as well as annexin V, is observed to modulate phase transition temperatures, indicating that peripheral protein binding may be a regulator for lateral heterogeneity in vivo. The partitioning of numerous signal protein anchors and full length proteins is investigated. We find Lo phase partitioning for several proteins assumed in the literature to be membrane raft associated, but observe deviations from this expectation for other proteins, including caveolin-1.

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Section: Resultssupporting

confidence: 83%

Temperature-dependent phase behavior and protein partitioning in giant plasma membrane vesicles

Johnson

Stinson

et al. 2010

Biochimica et Biophysica Acta (BBA) - Biomembranes

102

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“…The lipid suspension is vortexed and then passed 11 times through a polycarbonate filter with uniform 100 nm pores (Avanti Polar Lipids). For compositions of cholesterol/DOPC/bSM, lipids are extruded at a temperature above the lipid phase transition temperature, T m , using the lipid phase diagram of giant unilamellar vesicles (GUVs) for these lipid compositions as a reference to determine T m (32).…”

Section: Preparation Of Large Unilamellar Vesiclesmentioning

confidence: 99%

Asymmetric Structural Features in Single Supported Lipid Bilayers Containing Cholesterol and GM1 Resolved with Synchrotron X-Ray Reflectivity

Reich

Horton

Krause

et al. 2008

Biophysical Journal

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The cell membrane comprises numerous protein and lipid molecules capable of asymmetric organization between leaflets and liquid-liquid phase separation. We use single supported lipid bilayers (SLBs) to model cell membranes, and study how cholesterol and asymmetrically oriented ganglioside receptor G(M1) affect membrane structure using synchrotron x-ray reflectivity. Using mixtures of cholesterol, sphingomyelin, and 1,2-dioleoyl-sn-glycero-3-phosphocholine, we characterize the structure of liquid-ordered and liquid-disordered SLBs in terms of acyl-chain density, headgroup size, and leaflet thickness. SLBs modeling the liquid-ordered phase are 10 A thicker and have a higher acyl-chain electron density (rho(chain) = 0.33 e(-)/A(3)) compared to SLBs modeling the liquid-disordered phase, or pure phosphatidylcholine SLBs (rho(chain) = 0.28 e(-)/A(3)). Incorporating G(M1) into the distal bilayer leaflet results in membrane asymmetry and thickening of the leaflet of 4-9 A. The structural effect of G(M1) is more complex in SLBs of cholesterol/sphingomyelin/1,2-dioleoyl-sn-glycero-3-phosphocholine, where the distal chains show a high electron density (rho(chain) = 0.33 e(-)/A(3)) and the lipid diffusion constant is reduced by approximately 50%, as measured by fluorescence microscopy. These results give quantitative information about the leaflet asymmetry and electron density changes induced by receptor molecules that penetrate a single lipid bilayer.

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“…The cholesterol-binding capacity of caveolin-1 plays a key role in maintaining a stable balance of intracellular cholesterol, allowing caveolin-1 to act as a transporter that directs cholesterol efflux, selective uptake, and the delivery of newly synthesized cholesterol to the plasma membrane (Fielding, 2006). The membrane binding and lipid raft interactions of synthetic peptides derived from the CSD of the caveolin-1 protein (caveolin-1 scaffolding domain peptide, SDP) have been investigated (Horton et al, 2006;Benferhat et al, 2008).…”

Section: Introductionmentioning

confidence: 99%

Involvement of caveolin-1 in the Jak–Stat signaling pathway and infectious spleen and kidney necrosis virus infection in mandarin fish (Siniperca chuatsi)

Guo

Yang

et al. 2011

Molecular Immunology

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Caveolae, the major source of caveolin-1 protein, are specialized invaginated microdomains of the plasma membrane that act as organizing centers for signaling molecules in the immune system. In the present study, we report the cloning and characterization of caveolin-1 (mCav-1) from mandarin fish (Siniperca chuatsi) and study on the roles of mCav-1 in the fish Jak-Stat signaling pathway and in virus infection. The cDNA sequence of mCav-1 was 707bp in size, encoding a protein of 181 amino acids, which was different from the mammalian protein (178 amino acids). The deduced amino acid sequence of mCav-1 shared similar architecture with vertebrate caveolin-1 proteins, but mCav-1 lacked a phosphorylation site (y14). The major subcellular location of mCav-1 was in the caveolae, where the protein appeared to have major functions. Real-time PCR revealed that the expression of the mandarin fish Mx, IRF-1, SOCS1, and SOCS3 genes involved in the poly(I:C)-induced Jak-Stat signaling pathway was impaired by the mCav-1 scaffolding domain peptide (mSDP). In mandarin fish fry (MFF-1) cells, the protein levels of mCav-1 were markedly up-regulated at 12 and 24h post-infection with ISKNV (infectious spleen and kidney necrosis virus). In addition, ISKNV entry into MFF-1 cells was significantly inhibited by mSDP, and the inhibition was dose-dependent. Thus, ISKNV infection was apparently associated with mCav-1 protein and may utilize the caveolae-related endocytosis pathway. The findings reported here further our understanding of the function of caveolin-1 in the complex signal transduction network in fish immune systems and in the cellular entry mechanism of iridoviruses.

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Phase behavior and the partitioning of caveolin-1 scaffolding domain peptides in model lipid bilayers

Cited by 12 publications

References 56 publications

Temperature-dependent phase behavior and protein partitioning in giant plasma membrane vesicles

Temperature-dependent phase behavior and protein partitioning in giant plasma membrane vesicles

Asymmetric Structural Features in Single Supported Lipid Bilayers Containing Cholesterol and GM1 Resolved with Synchrotron X-Ray Reflectivity

Involvement of caveolin-1 in the Jak–Stat signaling pathway and infectious spleen and kidney necrosis virus infection in mandarin fish (Siniperca chuatsi)

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