ArticlePloS one2010
Silkworm coatomers and their role in tube expansion of posterior silkgland.
Article in PloS one, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 20 citations in OpenAlex.
- Silk_40K SNP array facilitates the genomic prediction of complex traits in silkworm (Bombyx mori).Journal of advanced research · 2026Article
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- DNA damage triggers tubular endoplasmic reticulum extension to promote apoptosis by facilitating ER-mitochondria signaling.Cell research · 2018Article
- Extracellular calumenin suppresses ERK1/2 signaling and cell migration by protecting fibulin-1 from MMP-13-mediated proteolysis.Oncogene · 2015Article
- Calumenin-15 facilitates filopodia formation by promoting TGF-β superfamily cytokine GDF-15 transcription.Cell death & disease · 2013Article
- BmCREC is an endoplasmic reticulum (ER) resident protein and required for ER/Golgi morphology.The Journal of biological chemistry · 2013Article
- A non-enzymatic function of Golgi glycosyltransferases: mediation of Golgi fragmentation by interaction with non-muscle myosin IIA.Glycobiology · 2013Article
- Expression and localization of silkworm adaptor protein complex-1 subunits, which were down-regulated post baculovirus infection.Molecular biology reports · 2012Article
- Article
- Defects in coatomer protein I (COPI) transport cause blood feeding-induced mortality in Yellow Fever mosquitoes.Proceedings of the National Academy of Sciences of the United States of America · 2011Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
10 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
backgroundCoat protein complex I (COPI) vesicles, coated by seven coatomer subunits, are mainly responsible for Golgi-to-ER transport. Silkworm posterior silkgland (PSG), a highly differentiated secretory tissue, secretes fibroin for silk production, but many physiological processes in the PSG cells await further investigation. METHODOLOGY/PRINCIPAL
findingsHere, to investigate the role of silkworm COPI, we cloned six silkworm COPI subunits (α, β, β', δ, ε, and ζ-COP), determined their peak expression in day 2 in fifth-instar PSG, and visualized the localization of COPI, as a coat complex, with cis-Golgi. By dsRNA injection into silkworm larvae, we suppressed the expression of α-, β'- and γ-COP, and demonstrated that COPI subunits were required for PSG tube expansion. Knockdown of α-COP disrupted the integrity of Golgi apparatus and led to a narrower glandular lumen of the PSG, suggesting that silkworm COPI is essential for PSG tube expansion. CONCLUSIONS/SIGNIFICANCE: The initial characterization reveals the essential roles of silkworm COPI in PSG. Although silkworm COPI resembles the previously characterized coatomers in other organisms, some surprising findings require further investigation. Therefore, our results suggest the silkworm as a model for studying intracellular transport, and would facilitate the establishment of silkworm PSG as an efficient bioreactor.
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