COPII‐mediated trafficking at the ER/ERGIC interface

Peotter, Jennifer L.; Kasberg, William; Pustova, Iryna; Audhya, Anjon

doi:10.1111/tra.12654

Cited by 114 publications

(122 citation statements)

References 139 publications

(212 reference statements)

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“…RINT1 was recently shown to be functionally associated with ERES that are involved in collagen export (Raote et al, 2018). More generally, the ERAS-ERAS relationship may be elaborated in cells that export large and complex cargoes from the ER (Peotter et al, 2019;Raote and Malhotra, 2019). In mammalian cells, retrograde COPI vesicles bud from ERGIC elements (Appenzeller-Herzog and Hauri, 2006;Hammond and Glick, 2000), which likely play a role in ERAS formation analogous to the role played by early Golgi cisternae in P. pastoris.…”

Section: Discussionmentioning

confidence: 99%

ER arrival sites associate with ER exit sites to create bidirectional transport portals

Chowdhury

Bhattacharjee

Casler

et al. 2020

Journal of Cell Biology

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COPI vesicles mediate Golgi-to-ER recycling, but COPI vesicle arrival sites at the ER have been poorly defined. We explored this issue using the yeast Pichia pastoris. ER arrival sites (ERAS) can be visualized by labeling COPI vesicle tethers such as Tip20. Our results place ERAS at the periphery of COPII-labeled ER export sites (ERES). The dynamics of ERES and ERAS are indistinguishable, indicating that these structures are tightly coupled. Displacement or degradation of Tip20 does not alter ERES organization, whereas displacement or degradation of either COPII or COPI components disrupts ERAS organization. We infer that Golgi compartments form at ERES and then produce COPI vesicles to generate ERAS. As a result, ERES and ERAS are functionally linked to create bidirectional transport portals at the ER–Golgi interface. COPI vesicles likely become tethered while they bud, thereby promoting efficient retrograde transport. In mammalian cells, the Tip20 homologue RINT1 associates with ERES, indicating possible conservation of the link between ERES and ERAS.

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Section: Discussionmentioning

confidence: 99%

ER arrival sites associate with ER exit sites to create bidirectional transport portals

Chowdhury

Bhattacharjee

Casler

et al. 2020

Journal of Cell Biology

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“…Properly folded proteins are secreted from the ER by coat protein complex II (COPII) vesicles to the Golgi apparatus, and then transported to the plasma membrane. Proteins such as hormones are secreted from the cell, while others, such as G protein coupled receptors (GPCRs), are expressed on the plasma membrane as cell-surface receptors (Peotter et al, 2019) (Figure 1).…”

Section: Er Stress and The Uprmentioning

confidence: 99%

Pathological Aspects of COVID-19 as a Conformational Disease and the Use of Pharmacological Chaperones as a Potential Therapeutic Strategy

Aoe

2020

Front. Pharmacol.

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Coronavirus disease 2019 (COVID-19), the seventh human coronavirus infectious disease, was first reported in Wuhan, China, in December 2019, followed by its rapid spread globally (251,059 deaths, on May 5, 2020, by Johns Hopkins University). An early clinical report showed that fever, cough, fatigue, sputum production, and myalgia were initial symptoms, with the development of pneumonia as the disease progressed. Increases in the level of serum liver enzymes, D-dimer, cardiac troponin I, and creatinine have been observed in severely ill patients, indicating that multiple organ failure had occurred in these cases. Lymphopenia and an increase in interleukin-6 (IL-6) were also observed. Although COVID-19 patients are administered glucocorticoid therapy to treat the excessive immune response to severe acute respiratory syndrome coronavirus-2 (SARS-CoV-2) infection, the efficacy of this form of therapy is unclear. Viremia is observed in severe cases, suggesting that in addition to type II alveolar epithelial cells, many cell types, such as vascular endothelial cells, cardiomyocytes, renal tubular cells, neuronal cells, and lymphocytes, may be damaged. The improvement of survival rates requires elucidation of the mechanism by which cellular damage occurs during viral infection. Cellular therapy, along with organ support systems such as oxygen therapy, artificial ventilation, extra corporeal membrane oxygenation and dialysis, as well as antiviral therapy, are required. Viral replication in infected host cells may perturb protein folding in the endoplasmic reticulum (ER), causing ER stress. Although an adaptive cellular response, i.e. the unfolded protein response, can compensate for the misfolded protein burden to some extent, continued viral proliferation may induce inflammation and cell death. Therefore, we propose that proteostasis dysfunction may cause conformational disorders in COVID-19. The application of pharmacological chaperone therapy to treat COVID-19 patients is additionally discussed.

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“…Exit from the ER additionally requires specific interactions of the cargo and COPII vesicular machinery components with specific ER lipids [27,29,38]. In mammalian cells, an intermediate compartment between the ER and the cis-Golgi has been defined and called ER-intermediate compartment (ERGIC) [39]. After successful ER-or ERGIC-exit, uncoated vesicles fuse with the cis-Golgi and then 'reach' the trans-Golgi network (TGN) via Golgi maturation [27,[40][41][42].…”

Section: Brief Account On the Trafficking Of Membrane Cargoes Via Conmentioning

confidence: 99%

Life and Death of Fungal Transporters Under the Challenge of Polarity

Dimou¹,

Diallinas²

2020

Preprint

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Eukaryotic plasma membrane (PM) transporters face critical challenges that are not widely present in prokaryotes. The two most important issues are proper subcellular traffic and targeting to the PM, and regulated endocytosis in response to physiological, developmental or stress signals. Sorting of transporters from their site of synthesis, the Endoplasmic Reticulum (ER), to the PM has been long thought, but not formally shown, to occur via the conventional Golgi-dependent vesicular secretory pathway. Endocytosis of specific eukaryotic transporters has been studied more systematically and shown to involve ubiquitination, internalization, and sorting to early endosomes, followed by turnover in the MVB/lysosomes/vacuole system. In specific cases internalized transporters have been shown to recycle back to the PM. However, the mechanisms of transporter forward trafficking and turnover have been overturned recently through systematic work in the model fungus Aspergillus nidulans. In this review we present evidence that shows that transporter traffic to the PM takes place through Golgi-bypass and transporter endocytosis operates via a mechanism that is distinct from that of recycling membrane cargoes essential for fungal growth. We discuss these findings in relation to adaptation to challenges imposed by cell polarity in fungi as well as in other eukaryotes and provide a rationale why transporters and possibly other housekeeping membrane proteins ‘avoid’ routes of polar trafficking.

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COPII‐mediated trafficking at the ER/ERGIC interface

Cited by 114 publications

References 139 publications

ER arrival sites associate with ER exit sites to create bidirectional transport portals

ER arrival sites associate with ER exit sites to create bidirectional transport portals

Pathological Aspects of COVID-19 as a Conformational Disease and the Use of Pharmacological Chaperones as a Potential Therapeutic Strategy

Life and Death of Fungal Transporters Under the Challenge of Polarity

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