The phosphatidylinositol 4-kinase PI4KIIIα is required for the recruitment of GBF1 to Golgi membranes

Dumaresq-Doiron, Karine; Savard, Marie-France; Akam, Salima; Costantino, Santiago; Lefrançois, Stéphane

doi:10.1242/jcs.055798

Cited by 50 publications

(43 citation statements)

References 33 publications

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“…On one hand, an involvement of the ERGIC implies a requirement for RAB1, which was the case for the formation of the assembly compartment, as well as for the production of HCV particles. In accordance, RAB1 and p115/USO1 were co-enriched in this compartment [43,62] . GBF1, an additional component of the ERGIC that activates small-sized GTPase ARF1 and, in turn, COPI-dependent traffic [43] , was also involved in the production of HCV particles [8] .…”

Section: Discussionsupporting

confidence: 55%

“…In accordance, RAB1 and p115/USO1 were co-enriched in this compartment [43,62] . GBF1, an additional component of the ERGIC that activates small-sized GTPase ARF1 and, in turn, COPI-dependent traffic [43] , was also involved in the production of HCV particles [8] . On the other hand, another feature of the ERGIC, the lectin ERGIC-53, was excluded from the assembly compartment.…”

Section: Discussionsupporting

confidence: 55%

“…As observed in TEM, the latter directly brought together membranes from the ER and the Golgi apparatus, which was consistent with an enrichment of this compartment in, respectively, Atlastin 1 [50][51][52] and GM130/GOLGA2 [41] , both reported to reorganize and/or maintain membranes of their organelle. In addition, an enrichment in both RAB1 and its GDI, like what was observed in the assembly compartment, has been reported to initiate a cascade of events involving GBF1, ARF1 and phosphatidylinositol 4-kinase Ⅲ alpha (PI4KⅢα) [43] , which may increase the local proportion of phosphatidylinositol 4-phosphate [63] and subvert endocytic trafficking [64] . In Huh-7.5 cells, this role is normally devoted to HCV NS5A that brings together PI4KⅢα and TBC1D20, an activator of RAB1 [65] .…”

Section: Discussionmentioning

confidence: 93%

“…We had previously observed that brefeldin A prevented the secretion of HCV by BHK-WNV cells, while it did not affect that of exosomes [8] . Brefeldin A is an inhibitor of GBF1 that activates small-sized GTPase ARF1 and, in turn, COPI-dependent traffic [43] . The effect of brefeldin A was consistent with HCV particles being released via a classical secretion path.…”

Section: Canx Recruits a Subset Of Hcv Proteins Into A Compartment Ofmentioning

confidence: 99%

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Assembly and release of infectious hepatitis C virus involving unusual organization of the secretory pathway

Triyatni

Berger

Saunier

2016

WJH

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Institutional review board statement: Approved the use of serum IgG of a patient cured from an HCV infection for in vitro studies (Hôpital and Institut Cochin, Paris).Institutional animal care and use committee statement: Not applicable.Conflict-of-interest statement: Saunier B, Triyatni M and Berger EA are co-inventors on NIH-owned patent #US 9052321 B2 on the HCV particle production system. Triyatni M et al . Unusual secretory pathway of hepatitis C virus in thin section transmission electron microscopy. These findings were compared with the JFH-1 strain/Huh-7.5 cell model. RESULTS:We found that CANX was necessary for the production of HCV particles by BHK-WNV cells. This process involved the recruitment of a subset of HCV proteins, detected by immunoglobulin of an HCV-cured patient, in a compartment of rearranged membranes bypassing the endoplasmic reticulum-Golgi intermediary compartment and surrounded by mitochondria. It also involved the maturation of N-linked glycans on HCV envelope proteins, which was required for assembly and/or secretion of HCV particles. The formation of this specialized compartment required RAB1; upon expression of HCV structural genes, this compartment developed large vesicles with viral particles. RAB1 and alpha-tubulin were required for the release of HCV particles. These cellular factors were also involved in the production of HCVcc in the JFH-1 strain/Huh-7.5 cell system, which involves HCV RNA replication. The secretion of HCV particles by BHK-WNV cells presents similarities with a pathway involving caspase-1; a caspase-1 inhibitor was found to suppress the production of HCV particles from a full-length genome. CONCLUSION:Prior activity of the WNV subgenomic replicon in BHK-21 cells promoted re-wiring of host factors for the assembly and release of infectious HCV in a caspase-1-dependent mechanism. Core tip: Our system for production of authentic infectious hepatitis C virus (HCV) in non-humanized, nonhepatic cells involves the rearrangement of inner cellular membranes triggered by the replication of flaviviruses. The present results suggest that this feature relies on the re-wiring of host factors that usually contribute to the secretion of glycoproteins to generate an unusual secretory pathway. This model offers a new way to study the properties of free HCV particles, i.e. , independently from lipoproteins.Triyatni M, Berger EA, Saunier B. Assembly and release of infectious hepatitis C virus involving unusual organization of the secretory pathway.

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Section: Discussionsupporting

confidence: 55%

Section: Discussionsupporting

confidence: 55%

Section: Discussionmentioning

confidence: 93%

Section: Canx Recruits a Subset Of Hcv Proteins Into A Compartment Ofmentioning

confidence: 99%

See 2 more Smart Citations

Assembly and release of infectious hepatitis C virus involving unusual organization of the secretory pathway

Triyatni

Berger

Saunier

2016

WJH

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“…Eps15 interacts with TGN-located AP-1 (Chi et al, 2008), and Rab1 activates a TGN-located molecule, PI-4 kinase III α, producing a high amount of PI4P (Dumaresq-Doiron et al, 2010). As a result, both Eps15 and PI4P-interacting GBF1 are retained on the TGN.…”

Section: Discussionmentioning

confidence: 99%

Localization of SMAP2 to the TGN and its Function in the Regulation of TGN Protein Transport

Funaki

Kon

Rönn

et al. 2011

Cell Struct. Funct.

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ABSTRACT. SMAP2 is an Arf GTPase-activating protein that is located and functions on early endosome membranes. In the present study, the trans-Golgi network (TGN) was verified as an additional site of SMAP2 localization based on its co-localization with various TGN-marker proteins. Mutation of specific stretches of basic amino acid residues abolished the TGN-localization of SMAP2. Over-expression of wild-type SMAP2, but not of the mutated SMAP2, inhibited the transport of vesicular stomatitis virus-G protein from the TGN to the plasma membrane. In contrast, this transport was enhanced in SMAP2 (-/-) cells characterized by increased levels of the activated form of Arf. SMAP2 therefore belongs to an ArfGAP subtype that resides on the TGN and functions as a negative regulator of vesicle budding from the organelle.

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Interaction between optineurin and Rab1a regulates autophagosome formation in neuroblastoma cells

Song

Jeon

Seo

et al. 2017

J of Neuroscience Research

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Optineurin (OPTN) is an autophagy receptor protein that has been implicated in glaucoma and amyotrophic lateral sclerosis. OPTN‐mediated autophagy is a complex process involving many autophagy‐regulating proteins. Autophagy plays a critical role in removing damaged organelles, intracellular pathogens, and protein aggregates to maintain cellular homeostasis. We identified Ypt1 as a novel interaction partner of OPTN by performing a large‐scale yeast‐human two‐hybrid assay. Coimmunoprecipitation assay showed that OPTN interacted with Rab1, the mammalian homolog of yeast Ypt1, in N2a mouse neuroblastoma cell line. We confirmed this interaction by confocal microscopy showing intracellular colocalization of the two proteins. We observed that a zinc finger domain of OPTN is important for Rab1a binding. Rab1a activity is also required for the binding with OPTN. The role of the OPTN‐Rab1a complex in neuronal autophagy was determined by measuring the translocation of microtubule‐associated protein light chain 3–EGFP to autophagosomes. In N2a cells, OPTN‐induced autophagosome formation was inhibited by Rab1a knockdown, indicating the important role of OPTN‐Rab1a interaction in neuronal autophagy processes. Similarly, in N2a cells overexpressing Rab1a, serum starvation–induced formation of autophagosome was enhanced, while OPTN knockdown reduced the Rab1a‐induced autophagy. These results show that the OPTN‐Rab1a complex modulates autophagosome formation in neuroblastoma cells.

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The phosphatidylinositol 4-kinase PI4KIIIα is required for the recruitment of GBF1 to Golgi membranes

Cited by 50 publications

References 33 publications

Assembly and release of infectious hepatitis C virus involving unusual organization of the secretory pathway

Assembly and release of infectious hepatitis C virus involving unusual organization of the secretory pathway

Localization of SMAP2 to the TGN and its Function in the Regulation of TGN Protein Transport

Interaction between optineurin and Rab1a regulates autophagosome formation in neuroblastoma cells

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