Pre- and post-golgi vacuoles operate in the transport of semliki forest virus membrane glycoproteins to the cell surface

Saraste, Jaakko; Kuismanen, Esa

doi:10.1016/0092-8674(84)90508-7

Cited by 508 publications

(410 citation statements)

References 57 publications

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“…4 shows that the recovery of activity was progressively slowed when temperatures decreased from 37°C (FR 1/2 ϭ 1 h) to 30°C (FR 1/2 ϭ 2 h) to 22°C (FR 1/2 ϭ 3.5 h). At 15°C, which typically blocks the ER-to-Golgi transition (20), the activity was recovered partially, up to 40% of the initial level (Fig. 4a).…”

Section: Resultsmentioning

confidence: 88%

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Function recovery after chemobleaching (FRAC): Evidence for activity silent membrane receptors on cell surface

Sun

Shikano

Xiong

et al. 2004

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

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Membrane proteins represent Ϸ30% of the proteome of both prokaryotes and eukaryotes. Unique to cell surface receptors is their biogenesis pathway, which involves vesicular trafficking from the endoplasmic reticulum through the Golgi apparatus and to the cell surface. Increasing evidence suggests specific regulation of biogenesis for different membrane receptors, hence affecting their surface expression. We report the development of a pulse-chase assay to monitor function recovery after chemobleaching (FRAC) to probe the transit time of the Kir2.1 K ؉ channel to reach the cell surface. Our results reveal that the channel activity is contributed by a small fraction of channel protein, providing evidence of activity-silent ''sleeping'' molecules on the cell surface. This method distinguishes molecular density from functional density, and the assay strategy is generally applicable to other membrane receptors. The ability of the reported method to access the biogenesis pathways in a high-throughput manner facilitates the identification and evaluation of molecules affecting receptor trafficking.covalent modification ͉ fluorescence recovery after photobleaching ͉ ion channels ͉ signaling ͉ trafficking

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Section: Resultsmentioning

confidence: 88%

“…3a and 4 a-c). It is known that lowering the temperature can stall the ER-to-Golgi or cis-to trans-Golgi transitions (20). In either case, only limited recovery should be observed, presumably caused by the vesicles in transit between trans-Golgi and the cell surface.…”

Section: Resultsmentioning

confidence: 99%

Function recovery after chemobleaching (FRAC): Evidence for activity silent membrane receptors on cell surface

Sun

Shikano

Xiong

et al. 2004

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

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“…Specifically, transport vesicles budding from the ER are not able to fuse with the Golgi apparatus at temperatures below 15°C, and transport beyond the TGN is inhibited at 20°C (55)(56)(57)(58). As an additional test of the proposal that GPIs are transported to the cell surface via a vesicular transport mechanism, we investigated the effect of lowered temperature on GPI transport to the cell surface.…”

Section: Fig 3 Analysis Of P10; H8 Is Mainly Located In the Mitochomentioning

confidence: 99%

Cell Surface Display and Intracellular Trafficking of Free Glycosylphosphatidylinositols in Mammalian Cells

Baumann¹,

Vidugirienė²,

Machamer³

et al. 2000

Journal of Biological Chemistry

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In addition to serving as membrane anchors for cell surface proteins, glycosylphosphatidylinositols (GPIs) can be found abundantly as free glycolipids in mammalian cells. In this study we analyze the subcellular distribution and intracellular transport of metabolically radiolabeled GPIs in three different cell lines. We use a variety of membrane isolation techniques (subcellular fractionation, plasma membrane vesiculation to isolate pure plasma membrane fractions, and enveloped viruses to sample cellular membranes) to provide direct evidence that free GPIs are not confined to their site of synthesis, the endoplasmic reticulum, but can redistribute to populate other subcellular organelles. Over short labeling periods (2.5 h), radiolabeled GPIs were found at similar concentration in all subcellular fractions with the exception of a mitochondria-enriched fraction where GPI concentration was low. Pulse-chase experiments over extended chase periods showed that although the total amount of cellular radiolabeled GPIs decreased, the plasma membrane complement of labeled GPIs increased. GPIs at the plasma membrane were found to populate primarily the exoplasmic leaflet as detected using periodate oxidation of the cell surface. Transport of GPIs to the cell surface was inhibited by Brefeldin A and blocked at 15°C, suggesting that GPIs are transported to the plasma membrane via a vesicular mechanism. The rate of transport of radiolabeled GPIs to the cell surface was found to be comparable with the rate of secretion of newly synthesized soluble proteins destined for the extracellular space.

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“…BHK21 cells were infected with the wild type SFV as described previously [17]. Pulse labeling with [ 35 S]methionine and immunoprecipitation with SFV-E2 speci¢c antiserum were performed according to Sariola et al [14].…”

Section: Viral Infection and Pulse-chase Experimentsmentioning

confidence: 99%

Inhibition of the membrane fusion machinery prevents exit from the TGN and proteolytic processing by furin

Band¹,

Määttä²,

Kääriäinen³

et al. 2001

FEBS Letters

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Pre- and post-golgi vacuoles operate in the transport of semliki forest virus membrane glycoproteins to the cell surface

Cited by 508 publications

References 57 publications

Function recovery after chemobleaching (FRAC): Evidence for activity silent membrane receptors on cell surface

Function recovery after chemobleaching (FRAC): Evidence for activity silent membrane receptors on cell surface

Cell Surface Display and Intracellular Trafficking of Free Glycosylphosphatidylinositols in Mammalian Cells

Inhibition of the membrane fusion machinery prevents exit from the TGN and proteolytic processing by furin

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