Brefeldin A: insights into the control of membrane traffic and organelle structure.

Klausner, Richard D.; Donaldson, Julie G.; Lippincott‐Schwartz, Jennifer

doi:10.1083/jcb.116.5.1071

Cited by 1,793 publications

(1,278 citation statements)

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“…3). As a further test of whether Cx47 mutants were localized in the ER, we treated bulk-selected cells for six hours with brefeldin A (BFA), a compound that disrupts the Golgi apparatus (Klausner et al 1992). As expected, BFA treatment dispersed the 58K staining to an ER-like pattern (compare untreated and treated 58K panels in Fig.…”

Section: Cx47 Mutants Localize To the Endoplasmic Reticulummentioning

confidence: 79%

Loss-of-function GJA12/Connexin47 mutations cause Pelizaeus–Merzbacher-like disease

Orthmann-Murphy

Enriquez

Abrams

et al. 2007

Molecular and Cellular Neuroscience

121

112

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Section: Cx47 Mutants Localize To the Endoplasmic Reticulummentioning

confidence: 79%

Loss-of-function GJA12/Connexin47 mutations cause Pelizaeus–Merzbacher-like disease

Orthmann-Murphy

Enriquez

Abrams

et al. 2007

Molecular and Cellular Neuroscience

121

112

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“…ARF binds to Golgi membranes in the GTP state via its amino-terminal myristate [3], and mediates the membrane recruitment of coatomer [4,5]. The GDP-GTP exchange on ARF is regulated by a membrane-associated guanine nucleotide exchange factor that is inhibited by the drug brefeldin A [6,7] which blocks membrane recruitment of coatomer and vesicular transport [8].…”

Section: Introductionmentioning

confidence: 99%

A role for ADP‐ribosylation factor 1, but not COP I, in secretory vesicle biogenesis from the trans‐Golgi network

Barr

Huttner

1996

FEBS Letters

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A synthetic N-myristoylated peptide corresponding to the amino-terminal domain of ADP-ribosylation factor 1 (ARF1) markedly increases, in a cell-free system using post-nuclear supernatant from PC12 cells, the biogenesis of constitutive secretory vesicles and immature secretory granules from the trans-Goigi network (TGN). The related N-myristoylated ARF4 peptide only weakly stimulates, and the non-myristoylated ARF1 and ARF4 peptides inhibit, the biogenesis of these secretory vesicles. In a modified cell-free system using TGN membranes, eoatomer-depleted cytosol supports the biogenesis of TGNderived secretory vesicles to the same extent as control cytosol. These results suggest a role for ARF1, but not the COP I coat, in secretory vesicle biogenesis from the TGN, possibly via the activation of phospholipase D. [10,11], the biogenesis of both CSVs and ISGs, collectively referred to as TGN-derived secretory vesicles, is inhibited by brefeldin A. If one extrapolates from the observations on the formation of cis-Golgi-derived vesicles to the biogenesis of TGN-derived secretory vesicles, the inhibition by brefeldin A would be indicative of an involvement of ARF in the latter process [12]. In the present study, we have examined a possible role of ARF in the biogenesis of TGN-derived secretory vesicles. In addition, we have addressed the related question of whether or not coatomer is required for the biogenesis of these vesicles. Materials and methods

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“…We also used several drugs that induce the ER stress response, a pathway induced by misfolded or unassembled proteins in the ER (Ma and Hendershot, 2001) that can lead to apoptosis if the stress is not alleviated (Nakagawa and Yuan, 2000). BFA is a fungal metabolite that blocks secretion and causes disassembly of the Golgi complex (Klausner et al, 1992) and with prolonged treatment induces apoptosis (Shao et al, 1996;Guo et al, 1998). Thapsigargin, which blocks the ER calcium pump, and DTT (a reducing agent) also activate the ER stress response.…”

Section: Apoptosis Is Impaired In Cells Expressing Caspaseresistant Gmentioning

confidence: 99%

Caspase-resistant Golgin-160 Disrupts Apoptosis Induced by Secretory Pathway Stress and Ligation of Death Receptors

Maag

Mancini

Rosen

et al. 2005

MBoC

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Golgin-160 is a coiled-coil protein on the cytoplasmic face of the Golgi complex that is cleaved by caspases during apoptosis. We assessed the sensitivity of cell lines stably expressing wild-type or caspase-resistant golgin-160 to several proapoptotic stimuli. Cells expressing a caspase-resistant mutant of golgin-160 were strikingly resistant to apoptosis induced by ligation of death receptors and by drugs that induce endoplasmic reticulum (ER) stress, including brefeldin-A, dithiothreitol, and thapsigargin. However, both cell lines responded similarly to other proapoptotic stimuli, including staurosporine, anisomycin, and etoposide. The caspase-resistant golgin-160 dominantly prevented cleavage of endogenous golgin-160 after ligation of death receptors or induction of ER stress, which could be explained by a failure of initiator caspase activation. The block in apoptosis in cells expressing caspase-resistant golgin-160 could not be bypassed by expression of potential caspase cleavage fragments of golgin-160, or by drug-induced disassembly of the Golgi complex. Our results suggest that some apoptotic signals (including those initiated by death receptors and ER stress) are sensed and integrated at Golgi membranes and that golgin-160 plays an important role in transduction of these signals. INTRODUCTIONThe Golgi complex is central to the regulation of membrane trafficking in eukaryotic cells. It is the primary site for sorting and processing of proteins undergoing both exocytosis and endocytosis (reviewed in Farquhar and Palade, 1998). Under normal conditions, the mammalian Golgi complex is a collection of stacks of cisternal membranes near the microtubule organizing center. Proteins traversing the secretory pathway enter the Golgi at the cis face, are processed as they pass through the Golgi stacks, and are sorted at the trans face into vesicles bound for their intended destinations. The trans-Golgi is also important in sorting proteins being endocytosed or cycling between the plasma membrane and intracellular membrane compartments. This affords the Golgi extensive communication with the rest of the cell and its surroundings, placing it in a prime position to sense and integrate information about the state of the cell and its environment.The structure of the Golgi is highly dynamic, allowing reversible disassembly during mitosis. Key secretory pathway proteins are phosphorylated in a cell cycle-dependent manner to stop membrane trafficking and disassemble the Golgi (reviewed in Rabouille and Jokitalo, 2003). This rearrangement from a single perinuclear organelle to dispersed vesiculated compartments is thought to ensure partitioning of the Golgi complex into both daughter cells during cytokinesis. When Golgi disassembly is prevented by addition of antibodies to Golgi reassembly and stacking protein of 65 kDa (GRASP65), cells complete S phase, but they are unable to enter mitosis. This mitotic block can be bypassed by disassembling the Golgi with drugs (Sutterlin et al., 2002). Once mitosis is complete, the Golgi...

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Brefeldin A: insights into the control of membrane traffic and organelle structure.

Cited by 1,793 publications

References 87 publications

Loss-of-function GJA12/Connexin47 mutations cause Pelizaeus–Merzbacher-like disease

Loss-of-function GJA12/Connexin47 mutations cause Pelizaeus–Merzbacher-like disease

A role for ADP‐ribosylation factor 1, but not COP I, in secretory vesicle biogenesis from the trans‐Golgi network

Caspase-resistant Golgin-160 Disrupts Apoptosis Induced by Secretory Pathway Stress and Ligation of Death Receptors

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