Brefeldin A, a drug that blocks secretion, prevents the assembly of non-clathrin-coated buds on Golgi cisternae

Orcl, Lelio; Tagaya, Mitsuo; Amherdt, M; Perrelet, Alain; Donaldson, Julie G.; Lippincott‐Schwartz, Jennifer; Klausner, Richard D.; Rothman, James E.

doi:10.1016/0092-8674(91)90273-2

Cited by 458 publications

(334 citation statements)

References 38 publications

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“…The staining obtained with the index human serum did not colocalize with the Golgi compartments, as determined by studies that used antibodies to golgin-97 ( Figure 1A; Griffith et al, 1997) and the marker of the ER/Golgi intermediate compartment p58 (Lahtinen et al, 1996;Figure 1B) or TGN38, a marker for the trans-Golgi network (TGN38; our unpublished results; Luzio et al, 1990). Brefeldin, a fungal toxin known to rapidly dissociate the Golgi complex (Orci et al, 1991) did not affect the morphology, size, or number of these structures (our unpublished results). The staining did not colocalize with clathrin-coated vesicles (Figure 1C), with the early endosomal protein EEA1 ( Figure 1D; Mu et al, 1995;Selak et al, 1999;Lawe et al, 2000), with the late endosomal protein rab9 (Lombardi et al, 1993; Figure 1E), with the peroxisome membrane protein PMP70 ( Figure 1F; Kamijo et al, 1990), with LAMP1 ( Figure 1G), a lysosome marker (Fukuda et al, 1988), or with caveolin (our unpublished results; Conrad et al, 1995;Song et al, 1995).…”

Section: Gw182 Is Localized To Cytoplasmic Specklesmentioning

confidence: 86%

A Phosphorylated Cytoplasmic Autoantigen, GW182, Associates with a Unique Population of Human mRNAs within Novel Cytoplasmic Speckles

Eystathioy

Chan

Tenenbaum

et al. 2002

MBoC

330

313

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A novel human cellular structure has been identified that contains a unique autoimmune antigen and multiple messenger RNAs. This complex was discovered using an autoimmune serum from a patient with motor and sensory neuropathy and contains a protein of 182 kDa. The gene and cDNA encoding the protein indicated an open reading frame with glycine-tryptophan (GW) repeats and a single RNA recognition motif. Both the patient's serum and a rabbit serum raised against the recombinant GW protein costained discrete cytoplasmic speckles designated as GW bodies (GWBs) that do not overlap with the Golgi complex, endosomes, lysosomes, or peroxisomes. The mRNAs associated with GW182 represent a clustered set of transcripts that are presumed to reside within the GW complexes. We propose that the GW ribonucleoprotein complex is involved in the posttranscriptional regulation of gene expression by sequestering a specific subset of gene transcripts involved in cell growth and homeostasis.

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Section: Gw182 Is Localized To Cytoplasmic Specklesmentioning

confidence: 86%

A Phosphorylated Cytoplasmic Autoantigen, GW182, Associates with a Unique Population of Human mRNAs within Novel Cytoplasmic Speckles

Eystathioy

Chan

Tenenbaum

et al. 2002

MBoC

330

313

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“…Coat protein binding is thought to favor formation of vesicles. BFA inhibits binding of certain coat proteins to membranes and causes dramatic formation of tubules from the Golgi, TGN, and endosomes Orci et al, 1991;Wood et al, 1991;Reaves and Banting, 1992). In contrast, activation of G proteins by A1F4 , GTP,yS, or mastoparan antagonizes BFA and promotes coat protein binding.…”

Section: Other Possible Functions For Arfmentioning

confidence: 99%

Role of heterotrimeric G proteins in membrane traffic.

Bomsel

Mostov

1992

MBoC

207

142

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“…Treatment of cells with BFA was used as a tool to examine the sub-Golgi localization of the enzyme. Owing to its effect of inhibiting the assembly of cytosolic coat proteins on target membranes, BFA inhibits vesicle formation [25,26] and leads to redistribution of proximal (cis-, medial-and trans-) Golgi membranes into the endoplasmic reticulum (ER), and of distal (TGN) membranes to the endosomal membrane system [27].…”

Section: Immunocytochemical Localization Of Galnac-tmentioning

confidence: 99%

GA2/GM2/GD2 synthase localizes to the trans-Golgi network of CHO-K1 cells

Giraudo

Fritz

Maccioni

1999

Biochemical Journal

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U D P - G a l N A c: l a c t o s y l c e r a m i d e / G M 3 / G D 3 β-1,4-N-a c e t y lgalactosaminyltransferase (GalNAc-T) transforms its acceptors into the gangliosides GA2, GM2 and GD2. It is well established that it is a Golgi-located glycosyltransferase, but its sub-Golgi localization is still unclear. We addressed this question in Chinese hamster ovary K1 cell clones stably transfected with a c-myc-tagged version of GalNAc-T which express the enzyme at different levels of activity. In these cell clones we examined the effect of brefeldin A (BFA) on the synthesis of glycolipids (in metabolic-labelling experiments) and on the sub-Golgi localization of the GalNAc-T (by immunocytochemistry). We found that in cell clones expressing moderate levels of activity, GalNAc-T immunoreactivity behaved as thetrans-Golgi network (TGN) marker mannose-6-P receptor (M6PR) both in BFA-treated and untreated cells, and that BFA completely blocked the synthesis of GM2, GM1 and GD1a. On the other hand, in cell clones expressing high levels of activity and treated with BFA, most GalNAc-T immunoreactivity redistributed to the endoplasmic reticulum, as did the medial-Golgi marker mannosidase II, and the synthesis of GM2, GM1 and GD1a was not completely blocked. These results indicate that GalNAc-T is a TGN-located enzyme and that the mechanism that localizes it to this compartment involves steps that, when saturated, lead to its mislocalization to the cis-, medial- or trans-Golgi. Changes of Golgi membrane properties by modification of local glycolipid composition due to the activity of the expressed enzyme were not the main cause of mislocalization, since it persists when glycolipid synthesis is inhibited with D,L-threo-1-phenyl-2-hexadecanoylamino-3-pyrrolidino-1-propanol-HCl.

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Brefeldin A, a drug that blocks secretion, prevents the assembly of non-clathrin-coated buds on Golgi cisternae

Cited by 458 publications

References 38 publications

A Phosphorylated Cytoplasmic Autoantigen, GW182, Associates with a Unique Population of Human mRNAs within Novel Cytoplasmic Speckles

A Phosphorylated Cytoplasmic Autoantigen, GW182, Associates with a Unique Population of Human mRNAs within Novel Cytoplasmic Speckles

Role of heterotrimeric G proteins in membrane traffic.

GA2/GM2/GD2 synthase localizes to the trans-Golgi network of CHO-K1 cells

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