Golgins and GRASPs: Holding the Golgi together

Ramirez, Irene Barinaga-Rementeria; Lowe, Martin

doi:10.1016/j.semcdb.2009.03.011

Cited by 127 publications

(73 citation statements)

References 146 publications

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“…Golgi fragmentation in apoptosis may depend on caspase 3 mediated cleavage of several membrane tethering factors involved in the structural organization of the Golgi, in particular GRASP65 and p115 [16,51,52]. We therefore examined whether motor neurons with Golgi fragmentation show reduced expression of these proteins.…”

Section: Resultsmentioning

confidence: 99%

Golgi fragmentation precedes neuromuscular denervation and is associated with endosome abnormalities in SOD1-ALS mouse motor neurons

Dis

Kuijpers

Haasdijk

et al. 2014

acta neuropathol commun

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BackgroundFragmentation of stacked cisterns of the Golgi apparatus into dispersed smaller elements is a feature associated with degeneration of neurons in amyotrophic lateral sclerosis (ALS) and some other neurodegenerative disorders. However, the role of Golgi fragmentation in motor neuron degeneration is not well understood.ResultsHere we use a SOD1-ALS mouse model (low-copy Gurney G93A-SOD1 mouse) to show that motor neurons with Golgi fragmentation are retrogradely labeled by intramuscularly injected CTB (beta subunit of cholera toxin), indicating that Golgi fragmentation precedes neuromuscular denervation and axon retraction. We further show that Golgi fragmentation may occur in the absence of and precede two other pathological markers, i.e. somatodendritic SOD1 inclusions, and the induction of ATF3 expression. In addition, we show that Golgi fragmentation is associated with an altered dendritic organization of the Golgi apparatus, does not depend on intact apoptotic machinery, and is facilitated in transgenic mice with impaired retrograde dynein-dependent transport (BICD2-N mice). A connection to altered dynein-dependent transport also is suggested by reduced expression of endosomal markers in neurons with Golgi fragmentation, which also occurs in neurons with impaired dynein function.ConclusionsTogether the data indicate that Golgi fragmentation is a very early event in the pathological cascade in ALS that is associated with altered organization of intracellular trafficking.

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Section: Resultsmentioning

confidence: 99%

Golgi fragmentation precedes neuromuscular denervation and is associated with endosome abnormalities in SOD1-ALS mouse motor neurons

Dis

Kuijpers

Haasdijk

et al. 2014

acta neuropathol commun

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show abstract

“…For example, Ypt6 interacts with subunits of the GARP tethering complex, acting on retrograde transport from the endosomes to the late Golgi (Siniossoglou andPelham 2001, Bonifacino andHierro 2011); Rab6 effectors interact with the retromer coat complex implicated in protein recycling from the endosomes to the Golgi (Wassmer et al 2009); COG8, a nonessential subunit of the intraGolgi-transport-mediating multisubunit tether COG, becomes essential in the absence of Ypt6 (Whyte and Munro 2001); Rab6 also is implicated in CopI-dependent and independent retrograde intra-Golgi and Golgi-to-ER pathways (Girod et al 1999, Smith et al 2009. Many golgins (proteins that influence Golgi organization) are known effectors of Rab6 (Ramirez and Lowe 2009). In A. nidulans RabC Rab6 localizes at the Golgi (Pantazopoulou and Penalva 2011).…”

Section: Rabcmentioning

confidence: 99%

The Golgi apparatus: insights from filamentous fungi

Pantazopoulou

2016

Mycologia

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Cargo passage through the Golgi, albeit an undoubtedly essential cellular function, is a mechanistically unresolved and much debated process. Although the main molecular players are conserved, diversification of the Golgi among different eukaryotic lineages is providing us with tools to resolve standing controversies. During the past decade the Golgi apparatus of model filamentous fungi, mainly Aspergillus nidulans, has been intensively studied. Here an overview of the most important findings in the field is provided. Golgi architecture and dynamics, as well as the novel cell biology tools that were developed in filamentous fungi in these studies, are addressed. An emphasis is placed on the central role the Golgi has as a crossroads in the endocytic and secretory-traffic pathways in hyphae. Finally the major advances that the A. nidulans Golgi biology has yielded so far regarding our understanding of key Golgi regulators, such as the Rab GTPases RabC Rab6 and RabE Rab11 , the oligomeric transport protein particle, TRAPPII, and the Golgi guanine nucleotide exchange factors of Arf1, GeaA GBF1/Gea1 and HypB BIG/Sec7 , are highlighted.

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“…Coiled-coil tethers are large, hydrophilic, homodimeric proteins comprising two globular heads connected by long coiled-coil domains. Owing to their large size, coiled-coil tethers can interact with vesicles over long distances (of more than 200 nm) [17], and the current model postulates that they facilitate the long-range sequestering of vesicles as the initial step in vesicle tethering [21-23]. MTCs, on the other hand, comprise a diverse family of proteins, with each member consisting of 3 to 10 subunits (Figure 2), resulting in an overall molecular weight of approximately 250 to 800 kDa [17].…”

Section: Classification Of Tethering Factorsmentioning

confidence: 99%

Membrane tethering

Chia¹,

Gleeson²

2014

F1000Prime Rep

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Membrane trafficking depends on transport vesicles and carriers docking and fusing with the target organelle for the delivery of cargo. Membrane tethers and small guanosine triphosphatases (GTPases) mediate the docking of transport vesicles/carriers to enhance the efficiency of the subsequent SNARE (soluble N-ethylmaleimide-sensitive factor attachment protein receptor)-mediated fusion event with the target membrane bilayer. Different classes of membrane tethers and their specific intracellular location throughout the endomembrane system are now well defined. Recent biochemical and structural studies have led to a deeper understanding of the mechanism by which membrane tethers mediate docking of membrane carriers as well as an appreciation of the role of tethers in coordinating the correct SNARE complex and in regulating the organization of membrane compartments. This review will summarize the properties and roles of membrane tethers of both secretory and endocytic systems.

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Golgins and GRASPs: Holding the Golgi together

Cited by 127 publications

References 146 publications

Golgi fragmentation precedes neuromuscular denervation and is associated with endosome abnormalities in SOD1-ALS mouse motor neurons

Golgi fragmentation precedes neuromuscular denervation and is associated with endosome abnormalities in SOD1-ALS mouse motor neurons

The Golgi apparatus: insights from filamentous fungi

Membrane tethering

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