Each Caveola Contains Multiple Glycosyl-phosphatidylinositol-anchored Membrane Proteins

Ying, Yun Shu; Anderson, Richard G. W.; Rothberg, Karen G.

doi:10.1101/sqb.1992.057.01.065

Cited by 82 publications

(71 citation statements)

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“…Endocytosis of crosslinked GPI-anchored proteins and gangliosides by caveolae has been reported in various cells (Parton, 1994;Keller et al, 1992;Ying et al, 1992;Parton et al, 1988;Tran et al, 1987;Montesano et al, 1982). The present study revealed that nonsialylated glycosphingolipids and sphingomyelin are also sequestered in caveolae after crosslinking.…”

Section: Discussionsupporting

confidence: 60%

GPI-anchored proteins, glycosphingolipids, and sphingomyelin are sequestered to caveolae only after crosslinking.

Fujimoto

1996

J Histochem Cytochem.

112

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GPI-anchored proteins, glpicosphingolipids, and sphhgomyelin are all enriched in the detergent-insoluble complex which has been suggested to be purified caveolae. I studied the relationship of the molecules with caveolae in cultured cells by i"unOcgt0chemical methods. In cells reacted with antibodies to various membrane proteins and lipids on ice and fmed More applying secondary antibodies, labeling did not show concentration in caveolae. In contrast, when cells were incubated with the primary and secondary antibodies on ice and then transferred to 37'C without fmtion, labeled Thy-1.2, p2-miaoglobulin, lactosyl ceramide, ceramide tetrahexose, Fomman antigen, and sphingomyelin became concentrated in caveolae, whereas labeled transferrin receptor did were sequestered in the same caveolae when crosslinked with not. Thy-1.2 and sphingolipids formed COIIUIIOII patches and

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Section: Discussionsupporting

confidence: 60%

GPI-anchored proteins, glycosphingolipids, and sphingomyelin are sequestered to caveolae only after crosslinking.

Fujimoto

1996

J Histochem Cytochem.

112

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“…RNA molecules, in particular noncoding RNAs, are present in the extracellular environment and body fluids either associated with proteins (90%) or within multivesicular bodies like exosomes (12,40). Extracellular RNA may interact with PrP present in the outer leaflet of the plasma membrane and catalyze the conversion of PrP C into PrP Sc either in cholesterol-rich microdomains (16,31,39) or along the endosomal recycling pathway (2,24), two sites hypothesized to sustain prion replication. our attention the use of beads for PMCA reactions.…”

Section: Discussionmentioning

confidence: 99%

Strain-Specific Role of RNAs in Prion Replication

Saá

Sferrazza

Ottenberg

et al. 2012

J Virol

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Several lines of evidence suggest that various cofactors may be required for prion replication. PrP binds to polyanions, and RNAs were shown to promote the conversion of PrP C into PrP Sc in vitro . In the present study, we investigated strain-specific differences in RNA requirement during in vitro conversion and the potential role of RNA as a strain-specifying component of infectious prions. We found that RNase treatment impairs PrP Sc -converting activity of 9 murine prion strains by protein misfolding cyclic amplification (PMCA) in a strain-specific fashion. While the addition of RNA restored PMCA conversion efficiency, the effect of synthetic polynucleotides or DNA was strain dependent, showing a different promiscuity of prion strains in cofactor utilization. The biological properties of RML propagated by PMCA under RNA-depleted conditions were compared to those of brain-derived and PMCA material generated in the presence of RNA. Inoculation of RNA-depleted RML in Tga20 mice resulted in an increased incidence of a distinctive disease phenotype characterized by forelimb paresis. However, this abnormal phenotype was not conserved in wild-type mice or upon secondary transmission. Immunohistochemical and cell panel assay analyses of mouse brains did not reveal significant differences between mice injected with the different RML inocula. We conclude that replication under RNA-depleted conditions did not modify RML prion strain properties. Our study cannot, however, exclude small variations of RML properties that would explain the abnormal clinical phenotype observed. We hypothesize that RNA molecules may act as catalysts of prion replication and that variable capacities of distinct prion strains to utilize different cofactors may explain strain-specific dependency upon RNA.

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“…More recently, the Taylor laboratory showed that depleting cells of the LRP1 receptor, a scavenger receptor that is internalized via clathrin-mediated endocytosis, blocks Cu 2+ -stimulated internalization of PrP c (Taylor and Hooper, 2007). However, it is not clear that this effect of LRP1 knockdown is due to a decrease in receptor internalization because LRP1 has also been shown to affect the biosynthetic trafficking of PrP c (Parkyn et al, 2008 (Ying et al, 1992), although other laboratories have not even detected the presence of caveolin in N2a cells (Marella et al, 2002;Shyng et al, 1994). Immunogold labeling also localized PrP c to caveolae in a CHO cell line that stably expresses hamster PrP c (Peters et al, 2003), and endogenous PrP c has also been detected in lipid rafts, as well as in clathrin-coated pits, in N2a cells (Sunyach et al, 2003).…”

Section: Introductionmentioning

confidence: 96%

Clathrin-independent internalization of normal cellular prion protein in neuroblastoma cells is associated with the Arf6 pathway

Kang

Zhao

Lovaas

et al. 2009

Journal of Cell Science

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To understand the role of clathrin-mediated endocytosis in the internalization of normal cellular prion protein (PrPc) in neuronal cells, N2a cells were depleted of clathrin by RNA interference. PrPc internalization via the constitutive endocytic pathway in the absence of Cu2+ and the stimulated pathway in the presence of Cu2+ were measured in both control and clathrin-depleted cells. Depletion of clathrin had almost no effect on the internalization of PrPc either in the presence or absence of Cu2+, in contrast to the marked reduction observed in transferrin uptake. By contrast, the internalization of PrPc was inhibited by the raft-disrupting drugs filipin and nystatin, and by the dominant-negative dynamin-1 mutant dynamin-1 K44A, both in the presence and absence of Cu2+. The internalized PrPc was found to colocalize with cargo that traffic in the Arf6 pathway and in large vacuoles in cells expressing the Arf6 dominant-active mutant. These results show that PrPc is internalized in a clathrin-independent pathway that is associated with Arf6.

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Each Caveola Contains Multiple Glycosyl-phosphatidylinositol-anchored Membrane Proteins

Cited by 82 publications

References 0 publications

GPI-anchored proteins, glycosphingolipids, and sphingomyelin are sequestered to caveolae only after crosslinking.

GPI-anchored proteins, glycosphingolipids, and sphingomyelin are sequestered to caveolae only after crosslinking.

Strain-Specific Role of RNAs in Prion Replication

Clathrin-independent internalization of normal cellular prion protein in neuroblastoma cells is associated with the Arf6 pathway

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