scholarly journals Lipid Rafts and Detergent-Resistant Membranes in Epithelial Keratinocytes

2014 ◽  
pp. 133-144 ◽  
Author(s):  
Kathleen P. McGuinn ◽  
Mỹ G. Mahoney
Keyword(s):  
Lipid Rafts ◽  
Detergent Resistant Membranes

scholarly journals Gag Regulates Association of Human Immunodeficiency Virus Type 1 Envelope with Detergent-Resistant Membranes

2006 ◽  
Vol 80 (11) ◽  
pp. 5292-5300 ◽  
Author(s):  
Jayanta Bhattacharya ◽  
Alexander Repik ◽  
Paul R. Clapham
Keyword(s):  
Human Immunodeficiency Virus ◽  
Lipid Rafts ◽  
Human Immunodeficiency Virus Type ◽  
Cytoplasmic Domain ◽  
Virus Particles ◽  
Immunodeficiency Virus ◽  
Detergent Resistant Membranes ◽  
Envelope Incorporation ◽  
Hiv 1

ABSTRACT Assembly of the human immunodeficiency virus type 1 (HIV-1) envelope glycoprotein on budding virus particles is important for efficient infection of target cells. In infected cells, lipid rafts have been proposed to form platforms for virus assembly and budding. Gag precursors partly associate with detergent-resistant membranes (DRMs) that are believed to represent lipid rafts. The cytoplasmic domain of the envelope gp41 usually carries palmitate groups that were also reported to confer DRM association. Gag precursors confer budding and carry envelope glycoproteins onto virions via specific Gag-envelope interactions. Thus, specific mutations in both the matrix domain of the Gag precursor and gp41 cytoplasmic domain abrogate envelope incorporation onto virions. Here, we show that HIV-1 envelope association with DRMs is directly influenced by its interaction with Gag. Thus, in the absence of Gag, envelope fails to associate with DRMs. A mutation in the p17 matrix (L30E) domain in Gag (Gag L30E) that abrogates envelope incorporation onto virions also eliminated envelope association with DRMs in 293T cells and in the T-cell line, MOLT 4. These observations are consistent with a requirement for an Env-Gag interaction for raft association and subsequent assembly onto virions. In addition to this observation, we found that mutations in the gp41 cytoplasmic domain that abrogated envelope incorporation onto virions and impaired infectivity of cell-free virus also eliminated envelope association with DRMs. On the basis of these observations, we propose that Gag-envelope interaction is essential for efficient envelope association with DRMs, which in turn is essential for envelope budding and assembly onto virus particles.

scholarly journals Analysis of Detergent-Resistant Membranes in Arabidopsis. Evidence for Plasma Membrane Lipid Rafts

2004 ◽  
Vol 137 (1) ◽  
pp. 104-116 ◽  
Author(s):  
Georg H.H. Borner ◽  
D. Janine Sherrier ◽  
Thilo Weimar ◽  
Louise V. Michaelson ◽  
Nathan D. Hawkins ◽  
...  
Keyword(s):  
Plasma Membrane ◽  
Lipid Rafts ◽  
Membrane Lipid ◽  
Plasma Membrane Lipid ◽  
Detergent Resistant Membranes

CLN3P, the Batten disease protein, localizes to membrane lipid rafts (detergent-resistant membranes)

2004 ◽  
Vol 317 (4) ◽  
pp. 988-991 ◽  
Author(s):  
Dinesh Rakheja ◽  
Srinivas B Narayan ◽  
Johanne V Pastor ◽  
Michael J Bennett
Keyword(s):  
Lipid Rafts ◽  
Batten Disease ◽  
Membrane Lipid ◽  
Disease Protein ◽  
Detergent Resistant Membranes

Active 3ʹ–5ʹ cyclic nucleotide phosphodiesterases are present in detergent-resistant membranes of mural granulosa cells

2017 ◽  
Vol 29 (4) ◽  
pp. 778 ◽  
Author(s):  
Annick Bergeron ◽  
Christine Guillemette ◽  
Marc-André Sirard ◽  
François J. Richard
Keyword(s):  
Cell Membrane ◽  
Lipid Rafts ◽  
Granulosa Cell ◽  
Granulosa Cells ◽  
Cell Membranes ◽  
Soluble Fraction ◽  
Cell Signalling ◽  
Membrane Microdomains ◽  
Dot Blot ◽  
Detergent Resistant Membranes

Lipids rafts are specialised membrane microdomains involved in cell signalling that can be isolated as detergent-resistant membranes (DRMs). The second messenger cyclic AMP (cAMP) has a central role in cell signalling in the ovary and its degradation is carried out by the phosphodiesterase (PDE) enzyme family. We hypothesised that PDEs could be functionally present in the lipid rafts of porcine mural granulosa cell membranes. PDE6C, PDE8A and PDE11A were detected by dot blot in the DRMs and the Triton-soluble fraction of the mural granulosa cells membrane and the cytosol. As shown by immunocytochemistry, PDEs showed clear immunostaining in mural granulosa cell membranes and the cytosol. Interestingly, cAMP–PDE activity was 18 times higher in the DRMs than in the Triton-soluble fraction of cell membranes and was 7.7 times higher in the cytosol than in the DRMs. cAMP–PDE activity in mural granulosa cells was mainly contributed by the PDE8 and PDE11 families. This study shows that PDEs from the PDE8 and PDE11 families are present in mural granulosa cells and that the cAMP–PDE activity is mainly contributed by the cytosol. In the cell membrane, the cAMP–PDE activity is mainly contributed by the DRMs. In addition, receptors for prostaglandin E2 and LH, two G-protein-coupled receptors, are present in lipid rafts and absent from the non-raft fraction of the granulosa cell membrane. These results suggest that in these cells, the lipid rafts exist as a cell-signalling platform and PDEs are one of the key enzyme families present in the raft.

scholarly journals Co‐localization of Hepatocellular Uptake Transporters in Detergent Resistant Membranes (Lipid Rafts)

2019 ◽  
Vol 33 (S1) ◽  
Author(s):  
Brianna Steiert ◽  
Jessica Y. Idowu ◽  
Larissa Dougherty ◽  
Bruno Hagenbuch
Keyword(s):  
Lipid Rafts ◽  
Detergent Resistant Membranes ◽  
Uptake Transporters

scholarly journals Organization on the plasma membrane of the retinitis pigmentosa protein RP2: investigation of association with detergent-resistant membranes and polarized sorting

2003 ◽  
Vol 372 (2) ◽  
pp. 427-433 ◽  
Author(s):  
J. Paul CHAPPLE ◽  
Celene GRAYSON ◽  
Alison J. HARDCASTLE ◽  
Tracey A. BAILEY ◽  
Karl MATTER ◽  
...  
Keyword(s):  
Plasma Membrane ◽  
Retinitis Pigmentosa ◽  
Cell Line ◽  
Lipid Rafts ◽  
Retinal Pigment ◽  
Significant Proportion ◽  
Wide Range ◽  
Detergent Resistant Membranes ◽  
Acylated Proteins

Mutations in the retinitis pigmentosa protein gene RP2 account for up to 15% of X-linked retinitis pigmentosa. RP2 is a novel protein of unknown function, which is targeted to the plasma membrane by dual N-terminal acyl-modification. Dual-acylated proteins are targeted to lipid rafts, and some are subject to polarized sorting. Therefore we investigated the organization of RP2 on the plasma membrane. Endogenous RP2 protein was predominantly localized at the plasma membrane, and exogenously expressed green-fluorescent-protein-tagged protein was also targeted to the membrane in a wide range of cultured cells. High levels of endogenous RP2 protein were present in HeLa cells and in the retinal pigment epithelium-derived cell line ARPE19. A significant proportion of RP2 in cultured neuroblastoma cells was associated with detergent-resistant membranes (DRMs), but much less than other dually acylated proteins (e.g. Lyn and Fyn). In contrast, the RP2-interacting protein Arl3 (ADP-ribosylation factor-like 3) was not found to be associated with DRMs. The association of RP2 with DRMs was cholesterol-dependent. In polarized epithelial cells in culture and in vivo, RP2 was present in both the apical and basolateral domains of the plasma membrane. These data show that RP2 is not specific to either domain, unlike some other dually acylated proteins. Interestingly, the level of RP2 protein increased in the epithelial cell line Caco-2 with differentiation and polarization. These data show that RP2 is present on the membrane of all cell types examined both in vitro and in vivo, and that RP2 associates with lipid rafts, suggesting a potential role for the protein in signal transduction.

Lipid Rafts, Detergent-Resistant Membranes, and Raft Targeting Signals

Physiology ◽  
2006 ◽  
Vol 21 (6) ◽  
pp. 430-439 ◽  
Author(s):  
Deborah A. Brown
Keyword(s):  
Lipid Rafts ◽  
Protein Function ◽  
Biological Membranes ◽  
Major Revision ◽  
Liquid Ordered ◽  
Cell Processes ◽  
Detergent Resistant Membranes ◽  
Targeting Signals

Lipid rafts are liquid-ordered (lo) phase microdomains proposed to exist in biological membranes. Rafts have been widely studied by isolating lo-phase detergent-resistant membranes (DRMs) from cells. Recent findings have shown that DRMs are not the same as preexisting rafts, prompting a major revision of the raft model. Nevertheless, raft-targeting signals identified by DRM analysis are often required for protein function, implicating rafts in a variety of cell processes.

scholarly journals Cholesterol-sensitive Modulation of Transcytosis

2007 ◽  
Vol 18 (6) ◽  
pp. 2057-2071 ◽  
Author(s):  
Julieta Leyt ◽  
Naomi Melamed-Book ◽  
Jean-Pierre Vaerman ◽  
Shulamit Cohen ◽  
Aryeh M. Weiss ◽  
...  
Keyword(s):  
Plasma Membrane ◽  
Lipid Rafts ◽  
Receptor Internalization ◽  
Cholesterol Depletion ◽  
Compensatory Mechanism ◽  
Membrane Domains ◽  
Caveolin 1 ◽  
Human Transferrin Receptor ◽  
Detergent Resistant Membranes ◽  
Tyrosine 14

Cholesterol-rich membrane domains (e.g., lipid rafts) are thought to act as molecular sorting machines, capable of coordinating the organization of signal transduction pathways within limited regions of the plasma membrane and organelles. The significance of these domains in polarized postendocytic sorting is currently not understood. We show that dimeric IgA stimulates the incorporation of its receptor into cholesterol-sensitive detergent-resistant membranes confined to the basolateral surface/basolateral endosomes. A fraction of human transferrin receptor was also found in basolateral detergent-resistant membranes. Disrupting these membrane domains by cholesterol depletion (using methyl-β-cyclodextrin) before ligand-receptor internalization caused depolarization of traffic from endosomes, suggesting that cholesterol in basolateral lipid rafts plays a role in polarized sorting after endocytosis. In contrast, cholesterol depletion performed after ligand internalization stimulated cargo transcytosis. It also stimulated caveolin-1 phosphorylation on tyrosine 14 and the appearance of the activated protein in dimeric IgA-containing apical organelles. We propose that cholesterol depletion stimulates the coupling of transcytotic and caveolin-1 signaling pathways, consequently prompting the membranes to shuttle from endosomes to the plasma membrane. This process may represent a unique compensatory mechanism required to maintain cholesterol balance on the cell surface of polarized epithelia.

scholarly journals Proteomic Profiling of Detergent Resistant Membranes (Lipid Rafts) of Prostasomes

2015 ◽  
Vol 14 (11) ◽  
pp. 3015-3022 ◽  
Author(s):  
Louise Dubois ◽  
Karl (K). Göran Ronquist ◽  
Bo Ek ◽  
Gunnar Ronquist ◽  
Anders Larsson
Keyword(s):  
Lipid Rafts ◽  
Proteomic Profiling ◽  
Detergent Resistant Membranes
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