Inactivation and activation of various membranal enzymes of the cholesterol biosynthetic pathway by digitonin.

Eilenberg, Haviva; Klinger, E; Przedecki, Fiorenza; Shechter, Ishaiahu

doi:10.1016/s0022-2275(20)38271-7

Cited by 11 publications

(2 citation statements)

References 36 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…To distinguish between these possibilities, we performed a digitonin permeabilization of the injected cells. Because digitonin selectively permeabilizes the plasma membrane (Eilenberg et al, 1989), this treatment allows the release of small vesicles but not the large anchored ER network. The diffuse Golgi staining evident in cells 3 h after injection of anti-p115 (Fig.…”

Section: Absence Of P115 Induces Apparent Copi-dependent Golgi Vesiculationmentioning

confidence: 99%

Evidence that Golgi structure depends on a p115 activity that is independent of the vesicle tether components giantin and GM130

Puthenveedu

Linstedt

2001

The Journal of Cell Biology

105

View full text Add to dashboard Cite

Inhibition of the putative coatomer protein I (COPI) vesicle tethering complex, giantin–p115–GM130, may contribute to mitotic Golgi breakdown. However, neither this, nor the role of the giantin–p115–GM130 complex in the maintenance of Golgi structure has been demonstrated in vivo. Therefore, we generated antibodies directed against the mapped binding sites in each protein of the complex and injected these into mammalian tissue culture cells. Surprisingly, the injected anti-p115 and antigiantin antibodies caused proteasome-mediated degradation of the corresponding antigens. Reduction of p115 levels below detection led to COPI-dependent Golgi fragmentation and apparent accumulation of Golgi-derived vesicles. In contrast, neither reduction of giantin below detectable levels, nor inhibition of p115 binding to GM130, had any detectable effect on Golgi structure or Golgi reassembly after cell division or brefeldin A washout. These observations indicate that inhibition of p115 can induce a mitotic-like Golgi disassembly, but its essential role in Golgi structure is independent of its Golgi-localized binding partners giantin and GM130.

show abstract

Section: Absence Of P115 Induces Apparent Copi-dependent Golgi Vesiculationmentioning

confidence: 99%

Evidence that Golgi structure depends on a p115 activity that is independent of the vesicle tether components giantin and GM130

Puthenveedu

Linstedt

2001

The Journal of Cell Biology

105

View full text Add to dashboard Cite

show abstract

“…Eukaryotic cells undergo extensive changes in their inin a Permeabilized Cell System tracellular architecture and physiology upon entry into NRK cells grown on Pronectin F coated glass coverslips mitosis. Some of the notable changes in mammalian were permeabilized with digitonin, a detergent that specells include condensation of DNA, fragmentation of the cifically binds to cholesterol (Eilenberg et al, 1989). This nuclear envelope and Golgi complex, depolymerization treatment resulted in preferential permeabilization of the of cytoplasmic microtubules, and a block in endocytic plasma membrane due to its proportionally higher choand exocytic protein transport (for a review, see Warren, lesterol content while intracellular organelles remained 1993).…”

Section: Golgi Fragmentation By Mitotic Extractmentioning

confidence: 99%

Signaling via Mitogen-Activated Protein Kinase Kinase (MEK1) Is Required for Golgi Fragmentation during Mitosis

Acharya

Mallabiabarrena

Acharya

et al. 1998

Cell

182

204

View full text Add to dashboard Cite

We have developed an assay using permeabilized cells to monitor fragmentation of the Golgi complex that occurs during mitosis. Golgi stacks, in permeabilized interphase normal rat kidney (NRK) cells, upon incubation with mitotic extracts undergo extensive fragmentation, and the fragmented Golgi membranes are dispersed throughout the cytoplasm. We find that the continued presence of p34cdc2, the mitosis initiation kinase, is not necessary for Golgi fragmentation. Instead, fragmentation depends on cytosolic mitogen-activated protein kinase kinase 1 (MEK1 or MAPKK1). However, the known cytoplasmic substrates for MEK1, ERK1, and ERK2 are not required for this process. Interestingly, we find a Golgi-associated ERK, which we propose as the likely target for MEK1 in Golgi fragmentation.

show abstract

Rationally Designed Inhibitors of Sterol Biosynthesis

Oehlschlager¹,

Czyzewska²

1992

Emerging Targets in Antibacterial and Antifungal Chemotherapy

View full text Add to dashboard Cite

Inactivation and activation of various membranal enzymes of the cholesterol biosynthetic pathway by digitonin.

Cited by 11 publications

References 36 publications

Evidence that Golgi structure depends on a p115 activity that is independent of the vesicle tether components giantin and GM130

Evidence that Golgi structure depends on a p115 activity that is independent of the vesicle tether components giantin and GM130

Signaling via Mitogen-Activated Protein Kinase Kinase (MEK1) Is Required for Golgi Fragmentation during Mitosis

Rationally Designed Inhibitors of Sterol Biosynthesis

Contact Info

Product

Resources

About