Genome-wide RNAi screening identifies human proteins with a regulatory function in the early secretory pathway
Abstract
The secretory pathway in mammalian cells has evolved to facilitate the transfer of cargo molecules to internal and cell surface membranes. Use of automated microscopy-based genome-wide RNA interference screens in cultured human cells allowed us to identify 554 proteins influencing secretion. Cloning, fluorescent-tagging and subcellular localization analysis of 179 of these proteins revealed that more than two-thirds localize to either the cytoplasm or membranes of the secretory and endocytic pathways. The depletion of 143 of them resulted in perturbations in the organization of the COPII and/or COPI vesicular coat complexes of the early secretory pathway, or the morphology of the Golgi complex. Network analyses revealed a so far unappreciated link between early secretory pathway function, small GTP-binding protein regulation, actin cytoskeleton organization and EGF-receptor-mediated signalling. This work provides an important resource for an integrative understanding of global cellular organization and regulation of the secretory pathway in mammalian cells.
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This explains the Golgi fragmentation phenotype seen here and previously upon KIF1C depletion.
“This explains the Golgi fragmentation phenotype seen here and previously upon KIF1C depletion (Simpson et al., 2012).”
From The Rab6-regulated KIF1C kinesin motor domain contributes to Golgi organization (2015) · cites this paper as Simpson et al., 2012
KIF1C depletion causes Golgi fragmentation in HeLa cells (previously reported).
“Depletion of KIF1C was previously reported to cause Golgi fragmentation in HeLa cells (Simpson et al., 2012).”
From The Rab6-regulated KIF1C kinesin motor domain contributes to Golgi organization (2015) · cites this paper as Simpson et al., 2012
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- Authors
- Simpson, J. C., Joggerst, B., Laketa, V., Verissimo, F., Cetin, C., Erfle, H., Bexiga, M. G., Singan, V. R., Hériché, J.-K., Neumann, B., Mateos, A., Blake, J., Bechtel, S., Benes, V., Wiemann, S., Ellenberg, J., & Pepperkok, R.
- Affiliations
- University College Dublin (IE)
- European Molecular Biology Laboratory (DE)
- Heidelberg University (DE)
- German Cancer Research Center (DE)
- Corresponding author
- Simpson, Jeremy C.
- Pepperkok, Rainer
- ORCID
- Venue
- Nature Cell Biology
- Published
- 2012-06-03
- Volume
- 14
- Issue
- 7
- Pages
- 764-774
- ISSN
- 1465-7392 (ISSN-L)
- 1476-4679
- OpenAlex
- W2080751376
- Cited by
- 186
- References
- 50
- Citations by year
- 2026: 5 · 2025: 5 · 2024: 8 · 2023: 9 · 2022: 9 · 2021: 9 · 2020: 11 · 2019: 15 · 2018: 9 · 2017: 13 · 2016: 24 · 2015: 21 · 2014: 21 · 2013: 22 · 2012: 5
- FWCI
- 10.45
- Type
- journal article
- Language
- en
- Open access
- closed
- Licence
- www.springer.com/tdm (tdm)
- Locations
- Nature Cell Biology (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular transport and secretion
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA Research and Splicing
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Fungal and yeast genetics research
- Keywords
- secretory pathway, early secretory pathway, protein secretion, Golgi apparatus, endocytic pathway, small GTPases, actin cytoskeleton, EGF receptor signalling, protein regulatory networks, membrane trafficking, human protein
- MeSH terms
- Cloning, Molecular, Endocytosis, Epidermal Growth Factor, Gene Expression Regulation, Golgi Apparatus, HeLa Cells, Humans, Actin Cytoskeleton, Microscopy, Fluorescence, Platelet-Derived Growth Factor, Recombinant Fusion Proteins, Time Factors, Transfection, Signal Transduction, Monomeric GTP-Binding Proteins, Protein Transport, Secretory Vesicles, Transport Vesicles, RNA Interference, Gene Regulatory Networks
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