Different Golgi ultrastructure across species and tissues: Implications under functional and pathological conditions, and an attempt at classification

Mirоnоv, Alexander A.; Сесорова, И. С.; Seliverstova, Elena V.; Beznoussenko, Galina V.

doi:10.1016/j.tice.2016.12.002

Cited by 31 publications

(41 citation statements)

References 158 publications

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“…The nature of this phenomenon remains unknown and could be subject to future studies that could also address the question of whether giantin oligomeric complexes are essential for the formation of large cisterna-cisterna communications. While the function of these internal Golgi "bridges" remains elusive, it was suggested that they could play a role in intra-Golgi trafficking and maintenance of the compact shape of the Golgi [113][114][115]. The alternative "short" intercisternal communications provided by GRASP65 oligomers seems efficient for Golgi compaction and positioning, but not sufficient for proper processing, because giantin depletion cardinally changes rate and quality of glycosylation, at least in HeLa cells [50].…”

Section: Discussionmentioning

confidence: 99%

“…In the meantime, the level of GRASP65 tetramer was significantly enhanced ( Figure 9A,B). We reasoned that giantin, and GRASP65 in absence of giantin, serve as the scaffold for Golgi intercisternal connections that seem necessary to maintain not only Golgi stacking but also rapid trafficking and processing [113][114][115]. Indeed, when we performed co-depletion of both giantin and GRASP65, Golgi perinuclear positioning and organization were substantially impaired ( Figure 9C-E).…”

Section: Is Grasp65 the Protein That May Compensate For The Lack Of Gmentioning

confidence: 99%

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Post-ER Stress Biogenesis of Golgi Is Governed by Giantin

Frisbie

Lushnikov

Krasnoslobodtsev

et al. 2019

Cells

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Background: The Golgi apparatus undergoes disorganization in response to stress, but it is able to restore compact and perinuclear structure under recovery. This self-organization mechanism is significant for cellular homeostasis, but remains mostly elusive, as does the role of giantin, the largest Golgi matrix dimeric protein. Methods: In HeLa and different prostate cancer cells, we used the model of cellular stress induced by Brefeldin A (BFA). The conformational structure of giantin was assessed by proximity ligation assay and atomic force microscopy. The post-BFA distribution of Golgi resident enzymes was examined by 3D SIM high-resolution microscopy. Results: We detected that giantin is rather flexible than an extended coiled-coil dimer and BFA-induced Golgi disassembly was associated with giantin monomerization. A fusion of the nascent Golgi membranes after BFA washout is forced by giantin re-dimerization via disulfide bond in its luminal domain and assisted by Rab6a GTPase. GM130-GRASP65-dependent enzymes are able to reach the nascent Golgi membranes, while giantin-sensitive enzymes appeared at the Golgi after its complete recovery via direct interaction of their cytoplasmic tail with N-terminus of giantin. Conclusion: Post-stress recovery of Golgi is conducted by giantin dimer and Golgi proteins refill membranes according to their docking affiliation rather than their intra-Golgi location.

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Section: Discussionmentioning

confidence: 99%

Section: Is Grasp65 the Protein That May Compensate For The Lack Of Gmentioning

confidence: 99%

Post-ER Stress Biogenesis of Golgi Is Governed by Giantin

Frisbie

Lushnikov

Krasnoslobodtsev

et al. 2019

Cells

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“…Similar results were obtained from cells treated with NMIIB or Rab6a siRNAs. We reasoned that giantin, and GRASP65 in absence of giantin, may serve as the materials for Golgi intercisternal connections that seem necessary to maintain not only Golgi stacking but also rapid trafficking and processing (Mironov, Sesorova et al, 2017, Rambourg, Clermont et al, 1993, Trucco, Polishchuk et al, 2004.…”

Section: Resultsmentioning

confidence: 99%

“…Second, giantin seems indispensable for the formation of a communication between Golgi stacks. While the function of these internal Golgi "bridges" remains elusive, it was suggested that they could play a role in intra-Golgi trafficking and maintenance of compact shape of Golgi (Mironov et al, 2017, Rambourg et al, 1993, Trucco et al, 2004. The alternative "short" intercisternal communication provided by GRASP65 oligomers seems efficient for Golgi compaction and positioning, but not sufficient for proper processing, because giantin depletion cardinally changes rate and quality of glycosylation (Koreishi et al, 2013).…”

Section: Discussionmentioning

confidence: 99%

Golgi Renaissance: the pivotal role of the largest Golgi protein giantin

Petrosyan

Manca

Casey

et al. 2018

Preprint

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Golgi undergoes disorganization in response to the drugs or alcohol, but it is able to restore compact structure under recovery. This self-organization mechanism remains mostly elusive, as does the role of giantin, the largest Golgi matrix dimeric protein. Here, we found that in cells treated with Brefeldin A (BFA) or ethanol (EtOH), Golgi disassembly is associated with giantin de-dimerization, which was restored to the dimer form after BFA or EtOH washout. Cells lacking giantin are disabled for the restoration of the classical ribbon Golgi, and they demonstrate altered trafficking of proteins to the cell surface. The fusion of the nascent Golgi membranes is mediated by the cross-membrane interaction of Rab6a GTPase and giantin. Giantin is involved in the formation of long intercisternal connections, which in giantin-depleted cells was replaced by the short bridges that formed via oligomerization of GRASP65. This phenomenon occurs in advanced prostate cancer cells, in which a fragmented Golgi phenotype is maintained by the dimerization of GRASP65. Thus, we provide a model of Golgi Renaissance, which is impaired in aggressive prostate cancer.

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“…Stress-dependent differences allow functional flexibility and adaptation to challenges to homeostasis. This is the likely reason for variations in Golgi morphology in different species and cell types (Mironov et al 2017; Mollenhauer and Morre 1978). The flattened, stacked Golgi structure described above is conserved in many species.…”

Section: Golgi Apparatus In Neuronsmentioning

confidence: 99%

Conserved Oligomeric Golgi and Neuronal Vesicular Trafficking

Climer

Hendrix²,

Lupashin

2017

Targeting Trafficking in Drug Development

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The conserved oligomeric Golgi (COG) complex is an evolutionary conserved multi-subunit vesicle tethering complex essential for the majority of Golgi apparatus functions: protein and lipid glycosylation and protein sorting. COG is present in neuronal cells, but the repertoire of COG function in different Golgi-like compartments is an enigma. Defects in COG subunits cause alteration of Golgi morphology, protein trafficking, and glycosylation resulting in human congenital disorders of glycosylation (CDG) type II. In this review we summa rize and critically analyze recent advances in the function of Golgi and Golgi-like compartments in neuronal cells and functions and dysfunctions of the COG complex and its partner proteins.

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Different Golgi ultrastructure across species and tissues: Implications under functional and pathological conditions, and an attempt at classification

Cited by 31 publications

References 158 publications

Post-ER Stress Biogenesis of Golgi Is Governed by Giantin

Post-ER Stress Biogenesis of Golgi Is Governed by Giantin

Golgi Renaissance: the pivotal role of the largest Golgi protein giantin

Conserved Oligomeric Golgi and Neuronal Vesicular Trafficking

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