Complete vesiculation of Golgi membranes and inhibition of protein transport by a novel sea sponge metabolite, ilimaquinone

Takizawa, Peter A.; Yucel, Jennifer K.; Veit, B; Faulkner, D. John; Deerinck, Thomas J.; Soto, Gabriel E.; Ellisman, Mark H.; Malhotra, Vivek

doi:10.1016/0092-8674(93)90638-7

Cited by 207 publications

(150 citation statements)

References 35 publications

Supporting

Mentioning

140

Contrasting

Order By: Relevance

“…To determine whether the recovery rate for GalNAc-T2-YFP is consistent with movement in vesicles, the cells were treated with IQ. This sponge metabolite has been extensively characterized by Malhotra and colleagues (Takizawa et al, 1993). They showed that the Golgi ribbon was converted into a collection of homogeneously sized vesicles, 90 nm in diameter.…”

Section: Discussionmentioning

confidence: 99%

“…As a positive control for Golgi vesicles, we used the well-characterized drug IQ, which converts the interphase Golgi apparatus into collections of small vesicles, 90 nm in diameter (Takizawa et al, 1993). By using the GalNAc-T2-YFP/CFP-Sec61␤ cell line, the Golgi was converted into a perinuclear haze, but there was no apparent effect on the ER.…”

Section: The Recovery Rate Of the Golgi Haze Is Similar To That Of Gomentioning

confidence: 99%

“…BODIPY ceramide was used as described by Sciaky et al (1997) and ilimaquinone as described by Takizawa et al (1993).…”

Section: Chemicalsmentioning

confidence: 99%

See 2 more Smart Citations

Rapid, Endoplasmic Reticulum-independent Diffusion of the Mitotic Golgi Haze

Axelsson

Warren

2004

MBoC

View full text Add to dashboard Cite

Early in mitosis, the mammalian Golgi apparatus disassembles, and fluorescence microscopy reveals Golgi clusters and an extensive, nonresolvable haze that either represents scattered vesicles or a merged endoplasmic reticulum (ER)-Golgi compartment. To help decide between these alternatives, we have carried out a combined microscopic and pharmacological analysis, by using a BS-C-1 cell line stably coexpressing ER and Golgi markers. Video fluorescence microscopy showed that these two organelles were morphologically distinguishable at all stages of mitosis, and photobleaching experiments showed that diffusion of the Golgi marker was unaffected by the presence of the ER. Fragmentation of the ER by using filipin III completely blocked diffusion of the ER marker but had no effect on the Golgi marker, unless it was first relocated to the ER by using brefeldin A. The Golgi haze was also studied using BODIPY ceramide. Its diffusion was slower in mitotic Golgi than in mitotic ER, but similar to that of a Golgi enzyme marker in the mitotic Golgi haze or in Golgi vesicles generated by ilimaquinone. Together, these results support the idea that the Golgi and the ER remain separate during mitosis and strongly suggest that Golgi markers move by vesicle diffusion, as opposed to lateral diffusion in continuous membranes. INTRODUCTIONThe status of the Golgi apparatus as an organelle has been the subject of a long-running debate that focused initially on the route taken by transiting cargo (cisternal maturation or vesicle-mediated transport; Glick and Malhotra, 1998;Pelham and Rothman, 2000) and, more recently, on the mechanisms of duplication and partitioning that underlie its biogenesis (Marsh and Howell, 2002;Munro, 2002). If the Golgi apparatus is responsible for its biogenesis, then it can be viewed as an autonomous organelle (Pelletier et al., 2002). If, on the other hand, it depends on the endoplasmic reticulum, then it can be viewed as a dependent organelle, which exists only as a consequence of ER functioning (Zaal et al., 1999;Bevis et al., 2002;Munro, 2002).Golgi partitioning during mitosis in animal cells has been particularly controversial, with models ranging from partitioning by Golgi elements themselves (Lucocq et al., 1989;Misteli and Warren, 1995;Jesch and Linstedt, 1998;Shima et al., 1998;Jesch et al., 2001;Jokitalo et al., 2001) to the partial or even complete merger of the Golgi with the ER, which then mediates the partitioning process (Thyberg and Moskalewski, 1992;Zaal et al., 1999;Kano et al., 2000;Terasaki, 2000). Although most biochemical experiments have yielded consistent results, suggesting a separation of the ER and Golgi during mitosis (Jesch and Linstedt, 1998;Farmaki et al., 1999;Jesch et al., 2001), microscopic experiments have often yielded contradictory results (Thyberg and Moskalewski, 1992;Shima et al., 1998;Zaal et al., 1999;Jokitalo et al., 2001).A particular issue has been the Golgi haze observed by fluorescence microscopy of mitotic cells. Breakdown and fragmentation of the Golgi ribbon a...

show abstract

Section: Discussionmentioning

confidence: 99%

Section: The Recovery Rate Of the Golgi Haze Is Similar To That Of Gomentioning

confidence: 99%

See 1 more Smart Citation

Rapid, Endoplasmic Reticulum-independent Diffusion of the Mitotic Golgi Haze

Axelsson

Warren

2004

MBoC

View full text Add to dashboard Cite

show abstract

“…Ilimaquinone (Takizawa et al, 1993) was from Vivek Malhotra (University of California, San Diego, La Jolla, CA). Soluble recombinant TNF-related apoptosis-inducing ligand (TRAIL) was from Calbiochem (San Diego, CA).…”

Section: Methodsmentioning

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

View full text Add to dashboard Cite

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...

show abstract

“…They found that IQ causes disassembly of the Golgi apparatus to form small vesicles with 60 -90 nm diameter (13) and reconstituted the assembly of Golgi stacks from vesiculated Golgi membranes (11). In the process of the assembly, NSF acts first to form larger vesicles of 300 nm diameter from small vesicles of 60 -90 nm, and p97 plays a role in the formation of Golgi cisternae from larger vesicles (11,12).…”

mentioning

confidence: 99%