Consequences of mutations in the genes of the ER export machinery COPII in vertebrates

Lu, Chung-Ling; Kim, Jin Oh

doi:10.1007/s12192-019-01062-3

Cited by 12 publications

(5 citation statements)

References 94 publications

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“…For example, COPII mediates nutrient availability in the metabolic control of liver protein and lipid trafficking in mammals. 31,32 Homozygous knockout mutants of COPII can induce embryonic lethality in mice and fish, 33,34 and in humans, COPII mutations cause diseases with distinct clinical features. 34 Recent studies demonstrated the diverse roles of COPII in several insects.…”

Section: Introductionmentioning

confidence: 99%

“…31,32 Homozygous knockout mutants of COPII can induce embryonic lethality in mice and fish, 33,34 and in humans, COPII mutations cause diseases with distinct clinical features. 34 Recent studies demonstrated the diverse roles of COPII in several insects. Studies showed that COPII is required for embryonic development in Drosophila melanogaster 35 and vitellogenesis in Aedes aegypti.…”

Section: Introductionmentioning

confidence: 99%

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Targeting coat protein II complex genes via RNA interference inhibits female adult feeding and reproductive development in the cabbage beetle Colaphellus bowringi

Tian

Guo

Zhu

et al. 2022

Pest Management Science

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BACKGROUND The cabbage beetle Colaphellus bowringi is a highly destructive cruciferous vegetable pest in Asia. This beetle is predominantly controlled by synthetic chemical pesticides, which leave pesticide residues on food and constitute a major hidden danger to human health. Based on preliminary research, we hypothesized that the coat protein II (COPII) complex, a primary coated vesicle that exports cargo molecules from the endoplasmic reticulum, is a promising novel target for the control of Colaphellus bowringi. RESULTS This study investigated whether disrupting COPII using RNA interference (RNAi) affects the growth and development of Colaphellus bowringi adults. The results showed that five COPII assembly genes, Sar1, Sec23, Sec24, Sec13, and Sec31, were uniformly expressed in multiple tissues of adult female Colaphellus bowringi. Injecting double‐stranded RNA (dsRNA) against each gene induced a high RNAi efficiency by approximately 55–99%, and considerably inhibited yolk deposition and ovarian growth. Moreover, knockdown of Sar1, Sec23 and Sec24 suppressed feeding and increased mortality to 26.67%, 46.67%, and 42.22%, respectively. This was partially due to the down‐regulation of insulin/mTOR‐associated nutritional pathways. The results indicate that silencing any of the five genes responsible for COPII complex assembly represses Juvenile hormone and ecdysone signaling pathways, suggesting that vesicle transport plays a vital role in the endocrine regulation of Colaphellus bowringi females. CONCLUSION This study suggests that the COPII complex could be a promising RNAi target for the management of Colaphellus bowringi, which would reduce our dependence on chemical pesticides for pest control. © 2022 Society of Chemical Industry.

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Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Targeting coat protein II complex genes via RNA interference inhibits female adult feeding and reproductive development in the cabbage beetle Colaphellus bowringi

Tian

Guo

Zhu

et al. 2022

Pest Management Science

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“…7, 8). COPII mutations are reported to cause ER stress, which has been interpreted as resulting from the accumulation of secretory proteins that cannot travel to the Golgi (33), but an additional cause might be an outcome of ERAD inhibition.…”

Section: Discussionmentioning

confidence: 99%

COP I and II dependent trafficking controls ER-associated degradation in mammalian cells

Ogen‐Shtern

Chang

Saad

et al. 2022

Preprint

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Misfolded proteins and components of the endoplasmic reticulum (ER) quality control and ER associated degradation (ERAD) machineries concentrate in the pericentriolar ER-derived quality control compartment (ERQC), suggesting it as a staging ground for ERAD. By tracking the chaperone calreticulin and an established ERAD substrate, asialoglycoprotein receptor H2a, we have now determined that the trafficking to the ERQC is reversible and recycling back to the ER is slower than the movement in the ER periphery. The dynamics suggest vesicular trafficking rather than diffusion. Indeed, using dominant negative mutants of ARF1 and Sar1 or the drugs Brefeldin A and H89, we observed that COPI inhibition causes accumulation in the ERQC and increased retrotranslocation and ERAD, whereas COPII inhibition has the opposite effect. Our results suggest that targeting of misfolded proteins to ERAD involves COPII-dependent transport to the ERQC and that they can be retrieved to the peripheral ER in a COPI-dependent manner.

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“…Finally, Sec13/Sec31 heterodimers complete membrane curvature and COPII vesicle formation (Fath et al, 2007;Stagg et al, 2008). Since their discovery in yeast cells, it has become clear through subsequent work that COPII components play important roles in the development of human diseases (Lu and Kim, 2020), so much that the work of their discoverer Randy Shekman has been acknowledged with the 2013 Nobel Prize in Physiology and Medicine. Indeed, mutations in genes encoding Sec23A lead to the accumulation of unsecreted procollagen within the ER and, consequently, to collagen deposition defects followed by skeletal and developmental alterations, as revealed in a rare genetic disease known as craniolenticulo-sutural dysplasia (LSD) (Boyadjiev et al, 2006).…”

Section: The Upr and The Multitasking Control Of Protein Foldingmentioning

confidence: 99%

ER exit pathways and the control of proteostasis: Crucial role of the UPR, COPII, and ER-phagy in the secretory pathway

Amodio¹,

Pagliara²,

Moltedo³

2022

Biocell

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The endoplasmic reticulum (ER) is the site of entry of all proteins that function in the secretory pathway including the extracellular environment. Because it controls the folding of newly synthesized secretory proteins, the ER is indispensable for the maintenance of proteostasis in the secretory pathway. Within the ER and, in part, in post-ER compartments, the quality control of protein folding is under the regulation of the unfolded protein response (UPR) pathways. The UPR strategy is to enhance protein folding, increase the ER degradation pathway of misfolded proteins, and allow the exit from the ER of only correctly folded proteins. The latter is controlled by the multimeric complex COPII, which also provides some of the components for ER-phagy the only route for the disposal of protein aggregates. In this overview, we wish to contribute to the introduction of new perspectives in the study of the mechanisms underlying the control of proteostasis within the secretory pathway.

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Consequences of mutations in the genes of the ER export machinery COPII in vertebrates

Cited by 12 publications

References 94 publications

Targeting coat protein II complex genes via RNA interference inhibits female adult feeding and reproductive development in the cabbage beetle Colaphellus bowringi

Targeting coat protein II complex genes via RNA interference inhibits female adult feeding and reproductive development in the cabbage beetle Colaphellus bowringi

COP I and II dependent trafficking controls ER-associated degradation in mammalian cells

ER exit pathways and the control of proteostasis: Crucial role of the UPR, COPII, and ER-phagy in the secretory pathway

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