A Novel Interaction of the Golgi Complex with the Vimentin Intermediate Filament Cytoskeleton

Gao, Ya-sheng; Sztul, Elizabeth

doi:10.1083/jcb.152.5.877

Cited by 100 publications

(90 citation statements)

References 86 publications

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“…Brefeldin A alters the architecture of vimentin networks Previous findings from our laboratory and others suggest that vimentin filaments regulate a subset of adaptor-based vesicular membrane transport events, as well as the position and structure of membranous organelles (Ameen et al, 2001;Faigle et al, 2000;Gao and Sztul, 2001;Styers et al, 2005;Styers et al, 2004;Toivola et al, 2004;Toivola et al, 2005). However, it remains unknown whether perturbations in the vesicular membrane transport machinery and organelle integrity lead to alterations in the architecture and function of vimentin networks.…”

Section: Resultsmentioning

confidence: 98%

“…For example, intermediate filaments are required for proper AP-3-mediated membrane protein sorting to lysosomes (Styers et al, 2004), polarized membrane protein delivery in epithelial tissues (Ameen et al, 2001;Toivola et al, 2004), and possibly the function of the vesicle fusion apparatus (Faigle et al, 2000). Furthermore, intermediate filaments also appear to be involved in lysosomal positioning and to interact with the Golgi complex (Gao and Sztul, 2001;Styers et al, 2004). This evidence indicates that the intermediate filament cytoskeleton modulates the maintenance and integrity of membranous compartments in the exocytic and endocytic routes.…”

Section: Introductionmentioning

confidence: 99%

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Architecture of the vimentin cytoskeleton is modified by perturbation of the GTPase ARF1

Styers

Kowalczyk

Faúndez

2006

Journal of Cell Science

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Intermediate filaments are required for proper membrane protein trafficking. However, it remains unclear whether perturbations in vesicular membrane transport result in changes in the architecture of the vimentin cytoskeleton. We find that treatment of cells with Brefeldin A, an inhibitor of specific stages of membrane transport, causes changes in the organization of vimentin filaments. These changes arise from movement of pre-existing filaments. Brefeldin A treatment also leads to alterations in the microtubule cytoskeleton. However, this effect is not observed in cells lacking intermediate filaments, indicating that microtubule bundling is downstream of perturbations in the vimentin cytoskeleton. Brefeldin A-induced changes in vimentin architecture are probably mediated through its effects on ADP-ribosylation factor 1 (ARF1). Expression of a dominant-negative mutant of ARF1 induces BFA-like modifications in vimentin morphology. The BFA-dependent changes in vimentin architecture occurred concurrently with the release of the ARF1-regulated adaptor complexes AP-3 and AP-1 from membranes and adaptor redistribution to vimentin networks. These observations indicate that perturbation of the vesicular membrane transport machinery lead to reciprocal changes in the architecture of vimentin networks.

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Section: Resultsmentioning

confidence: 98%

Section: Introductionmentioning

confidence: 99%

Architecture of the vimentin cytoskeleton is modified by perturbation of the GTPase ARF1

Styers

Kowalczyk

Faúndez

2006

Journal of Cell Science

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“…In addition, it has been shown that vimentin IF bind to formiminotransferase cyclodeaminase (FTCD), a peripheral component of the Golgi complex, both in vitro and in cells. Although this enzyme is known to be a bifunctional enzyme that catalyzes two sequential reactions in the histidine degradation pathway, it also links the Golgi complex to the IF cytoskeleton [45].…”

Section: Tethering and Positioningmentioning

confidence: 99%

Intermediate filaments: versatile building blocks of cell structure

Goldman

Grin

Mendez

et al. 2008

Current Opinion in Cell Biology

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SummaryCytoskeletal intermediate filaments (IF) are organized into a dynamic nano-fibrillar complex that extends throughout mammalian cells. This organization is ideally suited to their roles as response elements in the subcellular transduction of mechanical perturbations initiated at cell surfaces. IF also provide a scaffold for other types of signal transduction which together with molecular motors ferries signaling molecules from the cell periphery to the nucleus. Recent insights into their assembly highlight the importance of co-translation of their precursors, the hierarchical organization of their subunits in the formation of unit length filaments (ULF), and the linkage of ULF into mature apolar IF. Analyses by atomic force microscopy reveal that mature IF are flexible and can be stretched to over 300% of their length without breaking, suggesting that intrafilament subunits can slide past one another when exposed to mechanical stress and strain. IF also play a role in the organization of organelles by modulating their motility and providing anchorage sites within the cytoplasm.

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“…Vimentin-type intermediate filaments interact with lipid bilayers (60), and this interaction is mediated by the highly positively charged N-terminal domain (61). Vimentin has also been shown to be associated with both ER (62) and the Golgi apparatus (62)(63)(64). Vimentin forms a cage of intermediate filaments around cytosolic lipid droplets (65).…”

Section: Or Tip 47 (Not Shown)mentioning

confidence: 99%

A Phospholipase D-dependent Process Forms Lipid Droplets Containing Caveolin, Adipocyte Differentiation-related Protein, and Vimentin in a Cell-free System

Marchesan

Rutberg

Andersson

et al. 2003

Journal of Biological Chemistry

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We developed a microsome-based, cell-free system that assembles newly formed triglyceride (TG) into spherical lipid droplets. These droplets were recovered in the d < 1.055 g/ml fraction by gradient ultracentrifugation and were similar in size and appearance to those isolated from rat adipocytes and 3T3-L1 cells. Caveolin 1 and 2, vimentin, adipocyte differentiation-related protein, and the 78-kDa glucose regulatory protein were identified on the droplets from the cell-free system. The caveolin was soluble in 1% Triton X-100, as was the caveolin on lipid droplets from 3T3-L1 cells. The lipid droplets from the cell-free system, like those from 3T3-L1 cells, contained TG, diacylglycerol, phosphatidylcholine, phosphatidylethanolamine, and phosphatidylserine. The assembly of these TGcontaining structures was dependent on the rate of TG biosynthesis and required an activator present in the 160,000 ؋ g supernatant from homogenized rat adipocytes. The activator induced phospholipase D (PLD) activity, and its effect on the release of the TG-containing structures from the microsomes was inhibited by 1-butanol (but not 2-butanol) or 2,3-diphosphoglycerate. The activator could be replaced by a constitutively active PLD or phosphatidic acid. These results indicate that PLD and the formation of phosphatidic acid are important in the assembly of the TG-containing structures.Within the cell, triglycerides (TG) 1 are stored in cytosolic lipid droplets. Little is known about how these structures are assembled. Several proteins have been identified on their surface, including adipocyte differentiation-related protein (ADRP or adipophilin), perilipins (reviewed in Refs. 1 and 2), and caveolin (see Refs. 3-5 and reviewed in Refs. 2 and 6), but their roles in lipid droplet assembly are unknown.ADRP and perilipins are abundant on lipid droplets. ADRP is found mostly on smaller droplets; when overexpressed, it stimulates lipid droplet formation (7), suggesting a role in the assembly process. Perilipins are present on large lipid droplets (7) and have a central role in the turnover of TG within these structures (1, 8, 10), perhaps affording protection against hormone-sensitive lipase (11). Perilipin-null mice have smaller lipid droplets and a higher rate of basal lipolysis than wild-type mice and are resistant to diet-induced obesity (12).Caveolin is a 21-kDa membrane protein with a hairpin structure whose N and C termini face the cytosol (13, 14). In mammals, there are three caveolin genes. Caveolin 1 and 2 are expressed in adipocytes, whereas caveolin 3 is present in muscle. Caveolin plays a key role in intracellular lipid transport (15, 16), binding fatty acid (17), and transporting cholesterol (16) in a manner reminiscent of the way plasma apolipoproteins transport lipids in the blood (16,18).Phospholipase D (PLD) catalyzes the conversion of phosphatidylcholine to phosphatidic acid (PA) and appears to be important in intracellular transport and sorting processes (19 -22), either as an intracellular messenger or as a cone-shaped l...

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A Novel Interaction of the Golgi Complex with the Vimentin Intermediate Filament Cytoskeleton

Cited by 100 publications

References 86 publications

Architecture of the vimentin cytoskeleton is modified by perturbation of the GTPase ARF1

Architecture of the vimentin cytoskeleton is modified by perturbation of the GTPase ARF1

Intermediate filaments: versatile building blocks of cell structure

A Phospholipase D-dependent Process Forms Lipid Droplets Containing Caveolin, Adipocyte Differentiation-related Protein, and Vimentin in a Cell-free System

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