Microtubules and the organization of the Golgi complex

Thyberg, Johan; Moskalewski, Stanisław

doi:10.1016/s0014-4827(85)80032-x

Cited by 304 publications

(219 citation statements)

References 102 publications

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“…1b (i, iv), d (i, iv)]. In presence of NOC, the Golgi forms ''minstacks,'' as originally reported by Thyberg and Moskalewski [29] [ Fig. 1a (ii), c (ii)].…”

Section: Er-to-golgi Inhibitors Reduce Ifv Transportmentioning

confidence: 52%

“…Using the Golgi markers, GM130 and b-COP we found that virus infection results in Golgi fragmentation and dispersion. The breakdown and dispersal of the Golgi stacks has been reported to lower the efficiency of protein export [29] and can facilitate the replication of some intracellular pathogens [13]. Herpes Simplex Virus-1-induced Golgi fragmentation has been found to increase the efficiency of virion release into the extracellular space [5].…”

Section: Discussionmentioning

confidence: 99%

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Influenza infection modulates vesicular trafficking and induces Golgi complex disruption

et al. 2016

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Influenza A virus (IFV) replicates its genome in the nucleus of infected cells and uses the cellular protein transport system for genome trafficking from the nucleus to the plasma membrane. However, many details of the mechanism of this process, and its relationship to subsequent cytoplasmic virus trafficking, have not been elucidated. We examined the effect of nuclear transport inhibitors Leptomycin B (LB), 5,6 dichloro-1-b-D-ribofuranosyl-benzimidazole (DRB), the vesicular transport inhibitor Brefeldin A (BFA), the caspase inhibitor ZWEHD, and microtubule inhibitor Nocodazole (NOC) on virus replication and intracellular trafficking of viral nucleoprotein (NP) from the nucleus to the ER and Golgi. Also, we carried out complementary studies to determine the effect of IFV on intracellular membranes. Inhibition of the CRM1 and TAP-P15 nuclear transport pathways by DRB and LB blocked completely the export of virus. Inhibition of vesicular trafficking by BFA, NOC, and ZWEHD also affected influenza infection. Interestingly, IFV infection induced fragmentation of the Golgi complex resulting in diffuse distribution of large and small vesicles throughout the cytoplasm. Live-cell microscopy revealed expansion of Golgi localization signals indicating progressive dispersion of Golgi positive structures, resulting in the disassembly of the Golgi ribbon structure. Other vesicular components (Rab1b, ARF1 and GBF1) were also found to be required for IFV infection. Furthermore, the exact step at which IFV infection disrupts vesicle trafficking was identified as the ER-Golgi intermediate compartment. These findings suggest that IFV NP is trafficked from the nucleus via the CRM1 and TAP pathways. IFV modulates vesicular trafficking inducing disruption of the Golgi complex. These studies provide insight on the ways in which IFV affects intracellular trafficking of different host proteins and will facilitate identification of useful pharmaceutical targets to abrogate virus replication.

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“…1b (i, iv), d (i, iv)]. In presence of NOC, the Golgi forms ''minstacks,'' as originally reported by Thyberg and Moskalewski [29] [ Fig. 1a (ii), c (ii)].…”

Section: Er-to-golgi Inhibitors Reduce Ifv Transportmentioning

confidence: 52%

Section: Discussionmentioning

confidence: 99%

Influenza infection modulates vesicular trafficking and induces Golgi complex disruption

et al. 2016

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“…In interphase cells treated with the drug nocodazole to depolymerize microtubules, the Golgi readily fragments into ministacks that disperse throughout the cytosol (12). Simple drug washout leads to reformation of an intact, perinuclear Golgi ribbon.…”

Section: Premise 1: Lateral Fusion Within the Golgimentioning

confidence: 99%

How the Golgi works: A cisternal progenitor model

Pfeffer

2010

Proc. Natl. Acad. Sci. U.S.A.

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The Golgi complex is a central processing compartment in the secretory pathway of eukaryotic cells. This essential compartment processes more than 30% of the proteins encoded by the human genome, yet we still do not fully understand how the Golgi is assembled and how proteins pass through it. Recent advances in our understanding of the molecular basis for protein transport through the Golgi and within the endocytic pathway provide clues to how this complex organelle may function and how proteins may be transported through it. Described here is a possible model for transport of cargo through a tightly stacked Golgi that involves continual fusion and fission of stable, "like" subcompartments and provides a mechanism to grow the Golgi complex from a stable progenitor, in an ordered manner.

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“…Experiments from a number of laboratories have indicated that MTs and/or the MTOC play an important role in the structural integrity and location of the Golgi apparatus in cells [for reviews see Thyberg and Moskalewski, 1985;Kreis, 19901. Recent evidence suggests that the Golgi apparatus associates with a biochemically distinct subset of cellular MTs.…”

Section: Introductionmentioning

confidence: 99%

Disruption of the golgi apparatus with brefeldin a does not destabilize the associated detyrosinated microtubule network

Burgess

Skoufias

Wilson

1991

Cell Motil. Cytoskeleton

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Stable subsets of microtubules (MTs) are often enriched in detyrosinated a-tubulin. Recently it has been found that the Golgi apparatus is associated with a subset of relatively stable MTs and that detyrosinated MTs colocalize spatially and temporally with the Golgi apparatus in several cell lines. To determine whether the Golgi apparatus actively stabilizes associated MTs and thus allows their timedependent detyrosination, we have used the drug brefeldin A (BFA) to disrupt the Golgi apparatus and have monitored changes in the Golgi apparatus and MT populations using simultaneous immunofluorescence and fluorescent lectin microscopy. We found that although BFA caused the Golgi apparatus to completely redistribute to the endoplasmic reticulum (ER), the detyrosinated MTs were not disrupted and remained in a juxtanuclear region. By Western blot analysis we found that even after 6 h of continuous exposure of cells to BFA, there was no detectable reduction in the level of detyrosinated a-tubulin. Simultaneous treatment with nocodazole and BFA led to a complete disruption of all MTs and normal Golgi structureiorganization. Upon removal of nocodazole in the continued presence of BFA, we found that the detyrosinated MTs reformed in a compact juxtanuclear location in the absence of an intact Golgi complex. Finally, we found that the detyrosinated MTs colocalized precisely with a BFA-resistant structure that binds to the lectin, wheat germ agglutinin. We conclude that the juxtanuclear detyrosinated MTs are not actively stabilized by association with BFA-sensitive Golgi membranes. However, another closely associated structure which binds wheat germ agglutinin may serve to stabilize the juxtanuclear MTs. Alternatively, the MT organizing center (MTOC) and/or MT-associated proteins (MAPS) may organize and stabilize the juxtanuclear detyrosinated MTs.

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Microtubules and the organization of the Golgi complex

Cited by 304 publications

References 102 publications

Influenza infection modulates vesicular trafficking and induces Golgi complex disruption

Influenza infection modulates vesicular trafficking and induces Golgi complex disruption

How the Golgi works: A cisternal progenitor model

Disruption of the golgi apparatus with brefeldin a does not destabilize the associated detyrosinated microtubule network

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