Identification of a 200-kD, brefeldin-sensitive protein on Golgi membranes

Narula, Navneet; McMorrow, Isabel M.; Plopper, George E.; Doherty, J.; Matlin, KS; Burke, Brian; Stow, Jennifer L.

doi:10.1083/jcb.117.1.27

Cited by 114 publications

(77 citation statements)

References 47 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Dissociation of p200 from 2946 Lencer, de Almeida, Moe, Stow, Ausiello, and Madara Golgi membranes occurs rapidly upon exposure to BFA and precedes gross disruption ofGolgi morphology (36). We found that in T84 cells not treated with BFA mAbs against p200 labeled perinuclear structures consistent with the location of Golgi stacks (data not shown).…”

Section: Resultssupporting

confidence: 59%

“…For immunocytochemical localization of the Golgi associated protein p200 (36), monolayers grown on glass coverslips were incubated in HBSS with and without BFA for 30 min at 370C and fixed as described above. The fixed monolayers were permeabilized by incubation in 1% Triton X-100 in PBS for 20 min at 21'C, and then washed extensively in PBS containing 1% BSA (PBS/BSA).…”

Section: Introductionmentioning

confidence: 99%

See 1 more Smart Citation

Entry of cholera toxin into polarized human intestinal epithelial cells. Identification of an early brefeldin A sensitive event required for A1-peptide generation.

Lencer¹,

Almeida²,

Moe³

et al. 1993

J. Clin. Invest.

View full text Add to dashboard Cite

show abstract

Section: Resultssupporting

confidence: 59%

Section: Introductionmentioning

confidence: 99%

Entry of cholera toxin into polarized human intestinal epithelial cells. Identification of an early brefeldin A sensitive event required for A1-peptide generation.

Lencer¹,

Almeida²,

Moe³

et al. 1993

J. Clin. Invest.

View full text Add to dashboard Cite

show abstract

“…Although the precise structure of the 4.1B 200 variant has yet to be defined, we feel confident that this Golgi-associated constituent is a protein 4.1B because of the high specificity of our anti-4.1B-HP antibody, as evidenced by: (1) its failure to recognize other members of protein 4.1 family; (2) its failure to recognize any band in 4.1B-knockout tissues; and (3) the reduction of 4.1B 200 protein in siRNA-treated cells with a 4.1B-specific sequence. It is also interesting to note that a monoclonal antibody against canine liver Golgi membrane showed that a 200 kDa, BFA-sensitive protein was associated with the Golgi (Narula et al, 1992), although its identity and function are still uncertain. It has been shown that Na + /K + -ATPase transport from endoplasmic reticulum to Golgi depends on the Golgi spectrinankyrin G119 skeleton (Devarajan et al, 1997).…”

Section: Discussionmentioning

confidence: 99%

A Golgi-associated protein 4.1B variant is required for assimilation of proteins in the membrane

Kang

Wang

Zhang

et al. 2009

Journal of Cell Science

View full text Add to dashboard Cite

The archetypal membrane skeleton is that of the erythrocyte, consisting predominantly of spectrin, actin, ankyrin R and protein 4.1R. The presence in the Golgi of a membrane skeleton with a similar structure has been inferred, based on the identification of Golgi-associated spectrin and ankyrin. It has long been assumed that a Golgi-specific protein 4.1 must also exist, but it has not previously been found. We demonstrate here that a hitherto unknown form of protein 4.1, a 200 kDa 4.1B, is associated with the Golgi of Madin-Darby canine kidney (MDCK) and human bronchial epithelial (HBE) cells. This 4.1B variant behaves like a Golgi marker after treatment with Brefeldin A and during mitosis. Depletion of the protein in HBE cells by siRNA resulted in disruption of the Golgi structure and failure of Na+/K+-ATPase, ZO-1 and ZO-2 to migrate to the membrane. Thus, this newly identified Golgi-specific protein 4.1 appears to have an essential role in maintaining the structure of the Golgi and in assembly of a subset of membrane proteins.

show abstract

“…It also is supported by the finding that BFA-resistant Chinese hamster ovary (CHO) lines appear to produce an Arf1-type GEF (Melancon et al, 1997). Therefore, wherever Arf1 and its associated GEF are localized is the initial site of BFA action.BFA-sensitive GEFs are localized to the Golgi apparatus of mammalian cells (Narula et al, 1992;Mansour et al, 1999), as are Arf1p and Arf3p (Stearns et al, 1990;Peters et al, 1995). At least three Arf1p binding sites exist in the mammalian Golgi apparatus: the trans-Golgi network, where Arf1p is involved in the recruitment of the AP-1 adaptor complex of clathrin-coated vesicles (Traub et al, 1993;Boman et al, 2000); and the two compartments where COPI-coated vesicles are formed: the cis-cisternae (Oprins et al, 1993) and the ER-Golgi intermediate compartment (Griffiths et al, 1995;Martinez-Menarguez et al, 1999).…”

mentioning

confidence: 99%

Reevaluation of the Effects of Brefeldin A on Plant Cells Using Tobacco Bright Yellow 2 Cells Expressing Golgi-Targeted Green Fluorescent Protein and COPI Antisera

et al. 2002

View full text Add to dashboard Cite

Brefeldin A (BFA) causes a block in the secretory system of eukaryotic cells by inhibiting vesicle formation at the Golgi apparatus. Although this toxin has been used in many studies, its effects on plant cells are still shrouded in controversy. We have reinvestigated the early responses of plant cells to BFA with novel tools, namely, tobacco Bright Yellow 2 (BY-2) suspension-cultured cells expressing an in vivo green fluorescent protein-Golgi marker, electron microscopy of high-pressure frozen/freeze-substituted cells, and antisera against At ␥ -COP, a component of COPI coats, and AtArf1, the GTPase necessary for COPI coat assembly. The first effect of 10 g/mL BFA on BY-2 cells was to induce in Ͻ 5 min the complete loss of vesicle-forming At ␥ -COP from Golgi cisternae. During the subsequent 15 to 20 min, this block in Golgi-based vesicle formation led to a series of sequential changes in Golgi architecture, the loss of distinct Golgi stacks, and the formation of an endoplasmic reticulum (ER)-Golgi hybrid compartment with stacked domains. These secondary effects appear to depend in part on stabilizing intercisternal filaments and include the continued maturation of cis -and medial cisternae into trans -Golgi cisternae, as predicted by the cisternal progression model, the shedding of trans -Golgi network cisternae, the fusion of individual Golgi cisternae with the ER, and the formation of large ER-Golgi hybrid stacks. Prolonged exposure of the BY-2 cells to BFA led to the transformation of the ER-Golgi hybrid compartment into a sponge-like structure that does not resemble normal ER. Thus, although the initial effects of BFA on plant cells are the same as those described for mammalian cells, the secondary and tertiary effects have drastically different morphological manifestations. These results indicate that, despite a number of similarities in the trafficking machinery with other eukaryotes, there are fundamental differences in the functional architecture and properties of the plant Golgi apparatus that are the cause for the unique responses of the plant secretory pathway to BFA. INTRODUCTIONThe fungal toxin brefeldin A (BFA) has been used as an experimental tool to block secretion in a wide variety of eukaryotic cells (Fujiwara et al., 1988;Satiat-Jeunemaitre et al., 1996). In plants, it has been shown to block the secretion of cell wall polysaccharides and proteins (Driouich et al., 1993;Schindler et al., 1994;Kunze et al., 1995) as well as the transport of soluble proteins to the vacuole (Holwerda et al., 1992;Gomez and Chrispeels, 1993). In animals, the BFA-induced block of secretion is accompanied by a structural disruption of the secretory system, most notably involving the Golgi apparatus, which becomes extensively tubulated and eventually fuses with the endoplasmic reticulum (ER) (Sciaky et al., 1997;Hess et al., 2000). In contrast, the responses of plant cells to BFA range from a loss of ciscisternae and a concomitant increase in trans -cisternae to the accumulation of Golgi membranes in highly vesicul...

show abstract

Identification of a 200-kD, brefeldin-sensitive protein on Golgi membranes

Abstract: Abstract. A mAb A717 raised against canine liver

Cited by 114 publications

References 47 publications

Entry of cholera toxin into polarized human intestinal epithelial cells. Identification of an early brefeldin A sensitive event required for A1-peptide generation.

Entry of cholera toxin into polarized human intestinal epithelial cells. Identification of an early brefeldin A sensitive event required for A1-peptide generation.

A Golgi-associated protein 4.1B variant is required for assimilation of proteins in the membrane

Reevaluation of the Effects of Brefeldin A on Plant Cells Using Tobacco Bright Yellow 2 Cells Expressing Golgi-Targeted Green Fluorescent Protein and COPI Antisera

Contact Info

Product

Resources

About