The Golgi Apparatus and its Next-Door Neighbors

Nakano, Akihiko

doi:10.3389/fcell.2022.884360

Cited by 33 publications

(32 citation statements)

References 218 publications

(284 reference statements)

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“…Most de novo synthesized secretory and vacuolar proteins begin their journey from the ER, mediated by COPII-coated vesicles ( Barlowe et al, 1994 ; Bethune and Wieland, 2018 ). Subpopulations of ER- and Golgi-resident proteins cycle between the ER and Golgi, and COPI-coated vesicles mediate retrograde transport from the Golgi to the ER ( Matsuura-Tokita et al, 2006 ; Glick and Nakano, 2009 ; Ishii et al, 2016 ; Nakano, 2022 ). The COPI coat is also responsible for the intra-Golgi transport of Golgi-resident enzymes/proteins between Golgi cisternae.…”

Section: Discussionmentioning

confidence: 99%

Normal oil body formation in Marchantia polymorpha requires functional coat protein complex I proteins

2022

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Eukaryotic cells possess endomembrane organelles equipped with specific sets of proteins, lipids, and polysaccharides that are fundamental for realizing each organelle’s specific function and shape. A tightly regulated membrane trafficking system mediates the transportation and localization of these substances. Generally, the secretory/exocytic pathway is responsible for transporting cargo to the plasma membrane and/or the extracellular space. However, in the case of oil body cells in the liverwort Marchantia polymorpha, the oil body, a liverwort-unique organelle, is thought to be formed by secretory vesicle fusion through redirection of the secretory pathway inside the cell. Although their formation mechanism remains largely unclear, oil bodies exhibit a complex and bumpy surface structure. In this study, we isolated a mutant with spherical oil bodies through visual screening of mutants with abnormally shaped oil bodies. This mutant harbored a mutation in a coat protein complex I (COPI) subunit MpSEC28, and a similar effect on oil body morphology was also detected in knockdown mutants of other COPI subunits. Fluorescently tagged MpSEC28 was localized to the periphery of the Golgi apparatus together with other subunits, suggesting that it is involved in retrograde transport from and/or in the Golgi apparatus as a component of the COPI coat. The Mpsec28 mutants also exhibited weakened stiffness of the thalli, suggesting impaired cell–cell adhesion and cell wall integrity. These findings suggest that the mechanism of cell wall biosynthesis is also involved in shaping the oil body in M. polymorpha, supporting the redirection of the secretory pathway inward the cell during oil body formation.

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Section: Discussionmentioning

confidence: 99%

Normal oil body formation in Marchantia polymorpha requires functional coat protein complex I proteins

2022

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“…Then, the endocytic cargo α-factor is transported to the Vps21p-residing compartment dependent on GGA adaptors although whether they directly bind to the cargo is unclear, while Snc1p is transported to the PM. A recent study demonstrated that in plants the TGN has at least two subregions (zones) responsible for secretory and vacuolar trafficking (Nakano, 2022; Shimizu et al, 2021), and endocytic cargo transport via the Tlg2p sub-compartment might mediate this later zone. We recently reported that Vps9p, a GEF for Vps21p, is recruited to the TGN, and then transported to the endosome to activate Vps21p through Ent3p/5p-mediated vesicle transport (Nagano et al, 2019).…”

Section: Discussionmentioning

confidence: 99%

“…It is made available under a preprint (which was not certified by peer review) is the author/funder, who has granted bioRxiv a license to display the preprint in The copyright holder for this this version posted November 21, 2022. ; https://doi.org/10. 1101/2022…”

Section: Videomentioning

confidence: 99%

The yeast endocytic early/sorting compartment exists as an independent sub-compartment within thetrans-Golgi network

Toshima

Tsukahara

Nagano

et al. 2022

Preprint

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Although budding yeast has been extensively used as a model organism for studying organelle functions and intracellular vesicle trafficking, whether it possesses an independent endocytic early/sorting compartment that sorts endocytic cargos to the endo-lysosomal pathway or the recycling pathway has long been unclear. The structure and properties of the endocytic early/sorting compartment differ significantly between organisms; in plant cells the trans-Golgi network (TGN) serves this role, whereas in mammalian cells a separate intracellular structure performs this function. The yeast syntaxin homolog Tlg2p, widely localizing to the TGN and endosomal compartments, is presumed to act as a Q-SNARE for endocytic vesicles, but which compartment is the direct target for endocytic vesicles remained unanswered. Here we demonstrate by high-speed and high-resolution 4D imaging of fluorescently labeled endocytic cargos that the Tlg2p-residing compartment within the TGN functions as the early/sorting compartment. After arriving here, endocytic cargos are recycled to the plasma membrane or transported to the yeast Rab5-residing endosomal compartment through the pathway requiring the clathrin adaptors GGAs. Interestingly, Gga2p predominantly localizes at the Tlg2p-residing compartment, and the deletion of GGAs has little effect on another TGN region where Sec7p is present but suppresses dynamics of the Tlg2-residing early/sorting compartment, indicating that the Tlg2p- and Sec7p-residing regions are discrete entities in the mutant. Thus, the Tlg2p-residing region seems to serve as an early/sorting compartment, and function independently of the Sec7p-residing region within the TGN.

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“…Finally, MVBs are integrated in the cell membrane, a phenomenon that leads to the secretion of exosomes in the extracellular space via exocytosis. This step requires the involvement of soluble NSF attachment protein receptor (SNARE) proteins such as Ykt6, VAMP7, and syntaxin 1A (Syx1A), which have a key role in the fusion of MVBs with the cell membrane [ 29 , 30 ]. However, MVBs can be possibly led to lysosomes for degradation, or can be fused with autophagosomes [ 31 ].…”

Section: An Overview Of Extracellular Vesicle Biogenetic Mechanismsmentioning

confidence: 99%

The Emerging Role of Extracellular Vesicles and Autophagy Machinery in NASH—Future Horizons in NASH Management

Trifylli

Kriebardis

Koustas³

et al. 2022

IJMS

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Non-alcoholic fatty liver disease (NAFLD) is considered the most frequent chronic hepatic disease in the general population, while it is the first cause of liver transplantation in the US. NAFLD patients will subsequently develop non-alcoholic steatohepatitis (NASH), which is characterized by aberrant hepatocellular inflammation with or without the presence of fibrosis. The lack of specific biomarkers and therapeutic strategies makes non-alcoholic steatohepatitis (NASH) management a difficult task for clinicians. Extracellular vesicles (EVs) constitute a heterogenic population of vesicles produced by inward or outward plasma-membrane budding. There is an emerging connection between autophagy EVs production, via an unconventional non-degradative procedure. Alterations in the amount of the secreted EVs and the cargo they carry are also involved in the disease progression and development of NASH. Autophagy constitutes a multistep lysosomal degradative pathway that reassures cell homeostasis and survival under stressful conditions, such as oxygen and energy deprivation. It prevents cellular damage by eliminating defected proteins or nοn-functional intracellular organelles. At the same time, it reassures the optimal conditions for the cells via a different mechanism that includes the removal of cargo via the secretion of EVs. Similarly, autophagy machinery is also associated with the pathogenetic mechanism of NAFLD, while it has a significant implication for the progression of the disease and the development of NASH. In this review, we will shed light on the interplay between autophagy and EVs in NASH, the emerging connection of EVs production with the autophagy pathway, and their possible manipulation for developing future therapeutic strategies for NASH.

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The Golgi Apparatus and its Next-Door Neighbors

Cited by 33 publications

References 218 publications

Normal oil body formation in Marchantia polymorpha requires functional coat protein complex I proteins

Normal oil body formation in Marchantia polymorpha requires functional coat protein complex I proteins

The yeast endocytic early/sorting compartment exists as an independent sub-compartment within thetrans-Golgi network

The Emerging Role of Extracellular Vesicles and Autophagy Machinery in NASH—Future Horizons in NASH Management

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