Genome-wide siRNA screen reveals amino acid starvation-induced autophagy requires SCOC and WAC
Autophagy is a catabolic process by which cytoplasmic components are sequestered and transported by autophagosomes to lysosomes for degradation, enabling recycling of these components and providing cells with amino acids during starvation. It is a highly regulated process and its deregulation contri...
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| Published in | The EMBO journal Vol. 31; no. 8; pp. 1931 - 1946 |
|---|---|
| Main Authors | , , , , , , |
| Format | Journal Article |
| Language | English |
| Published |
Chichester, UK
John Wiley & Sons, Ltd
18.04.2012
Nature Publishing Group UK Springer Nature B.V Nature Publishing Group |
| Subjects | |
| Online Access | Get full text |
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| Abstract | Autophagy is a catabolic process by which cytoplasmic components are sequestered and transported by autophagosomes to lysosomes for degradation, enabling recycling of these components and providing cells with amino acids during starvation. It is a highly regulated process and its deregulation contributes to multiple diseases. Despite its importance in cell homeostasis, autophagy is not fully understood. To find new proteins that modulate starvation‐induced autophagy, we performed a genome‐wide siRNA screen in a stable human cell line expressing GFP–LC3, the marker‐protein for autophagosomes. Using stringent validation criteria, our screen identified nine novel autophagy regulators. Among the hits required for autophagosome formation are SCOC (short coiled‐coil protein), a Golgi protein, which interacts with fasciculation and elongation protein zeta 1 (FEZ1), an ULK1‐binding protein. SCOC forms a starvation‐sensitive trimeric complex with UVRAG (UV radiation resistance associated gene) and FEZ1 and may regulate ULK1 and Beclin 1 complex activities. A second candidate WAC is required for starvation‐induced autophagy but also acts as a potential negative regulator of the ubiquitin‐proteasome system. The identification of these novel regulatory proteins with diverse functions in autophagy contributes towards a fuller understanding of autophagosome formation.
A genome‐wide siRNA screen identifies autophagy regulators. The Golgi protein SCOC regulates the interaction between ULK1 kinase and the Beclin 1 complexes in a nutrient‐dependent manner; WAC enhances starvation‐induced autophagy, while inhibiting the ubiquitin‐proteasome system. |
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| AbstractList | Autophagy is a catabolic process by which cytoplasmic components are sequestered and transported by autophagosomes to lysosomes for degradation, enabling recycling of these components and providing cells with amino acids during starvation. It is a highly regulated process and its deregulation contributes to multiple diseases. Despite its importance in cell homeostasis, autophagy is not fully understood. To find new proteins that modulate starvation‐induced autophagy, we performed a genome‐wide siRNA screen in a stable human cell line expressing GFP–LC3, the marker‐protein for autophagosomes. Using stringent validation criteria, our screen identified nine novel autophagy regulators. Among the hits required for autophagosome formation are SCOC (short coiled‐coil protein), a Golgi protein, which interacts with fasciculation and elongation protein zeta 1 (FEZ1), an ULK1‐binding protein. SCOC forms a starvation‐sensitive trimeric complex with UVRAG (UV radiation resistance associated gene) and FEZ1 and may regulate ULK1 and Beclin 1 complex activities. A second candidate WAC is required for starvation‐induced autophagy but also acts as a potential negative regulator of the ubiquitin‐proteasome system. The identification of these novel regulatory proteins with diverse functions in autophagy contributes towards a fuller understanding of autophagosome formation.
A genome‐wide siRNA screen identifies autophagy regulators. The Golgi protein SCOC regulates the interaction between ULK1 kinase and the Beclin 1 complexes in a nutrient‐dependent manner; WAC enhances starvation‐induced autophagy, while inhibiting the ubiquitin‐proteasome system. Autophagy is a catabolic process by which cytoplasmic components are sequestered and transported by autophagosomes to lysosomes for degradation, enabling recycling of these components and providing cells with amino acids during starvation. It is a highly regulated process and its deregulation contributes to multiple diseases. Despite its importance in cell homeostasis, autophagy is not fully understood. To find new proteins that modulate starvation-induced autophagy, we performed a genome-wide siRNA screen in a stable human cell line expressing GFP-LC3, the marker-protein for autophagosomes. Using stringent validation criteria, our screen identified nine novel autophagy regulators. Among the hits required for autophagosome formation are SCOC (short coiled-coil protein), a Golgi protein, which interacts with fasciculation and elongation protein zeta 1 (FEZ1), an ULK1-binding protein. SCOC forms a starvation-sensitive trimeric complex with UVRAG (UV radiation resistance associated gene) and FEZ1 and may regulate ULK1 and Beclin 1 complex activities. A second candidate WAC is required for starvation-induced autophagy but also acts as a potential negative regulator of the ubiquitin-proteasome system. The identification of these novel regulatory proteins with diverse functions in autophagy contributes towards a fuller understanding of autophagosome formation. Autophagy is a catabolic process by which cytoplasmic components are sequestered and transported by autophagosomes to lysosomes for degradation, enabling recycling of these components and providing cells with amino acids during starvation. It is a highly regulated process and its deregulation contributes to multiple diseases. Despite its importance in cell homeostasis, autophagy is not fully understood. To find new proteins that modulate starvation-induced autophagy, we performed a genome-wide siRNA screen in a stable human cell line expressing GFP-LC3, the marker-protein for autophagosomes. Using stringent validation criteria, our screen identified nine novel autophagy regulators. Among the hits required for autophagosome formation are SCOC (short coiled-coil protein), a Golgi protein, which interacts with fasciculation and elongation protein zeta 1 (FEZ1), an ULK1-binding protein. SCOC forms a starvation-sensitive trimeric complex with UVRAG (UV radiation resistance associated gene) and FEZ1 and may regulate ULK1 and Beclin 1 complex activities. A second candidate WAC is required for starvation-induced autophagy but also acts as a potential negative regulator of the ubiquitin-proteasome system. The identification of these novel regulatory proteins with diverse functions in autophagy contributes towards a fuller understanding of autophagosome formation. [PUBLICATION ABSTRACT] Autophagy is a catabolic process by which cytoplasmic components are sequestered and transported by autophagosomes to lysosomes for degradation, enabling recycling of these components and providing cells with amino acids during starvation. It is a highly regulated process and its deregulation contributes to multiple diseases. Despite its importance in cell homeostasis, autophagy is not fully understood. To find new proteins that modulate starvation-induced autophagy, we performed a genome-wide siRNA screen in a stable human cell line expressing GFP-LC3, the marker-protein for autophagosomes. Using stringent validation criteria, our screen identified nine novel autophagy regulators. Among the hits required for autophagosome formation are SCOC (short coiled-coil protein), a Golgi protein, which interacts with fasciculation and elongation protein zeta 1 (FEZ1), an ULK1-binding protein. SCOC forms a starvation-sensitive trimeric complex with UVRAG (UV radiation resistance associated gene) and FEZ1 and may regulate ULK1 and Beclin 1 complex activities. A second candidate WAC is required for starvation-induced autophagy but also acts as a potential negative regulator of the ubiquitin-proteasome system. The identification of these novel regulatory proteins with diverse functions in autophagy contributes towards a fuller understanding of autophagosome formation.Autophagy is a catabolic process by which cytoplasmic components are sequestered and transported by autophagosomes to lysosomes for degradation, enabling recycling of these components and providing cells with amino acids during starvation. It is a highly regulated process and its deregulation contributes to multiple diseases. Despite its importance in cell homeostasis, autophagy is not fully understood. To find new proteins that modulate starvation-induced autophagy, we performed a genome-wide siRNA screen in a stable human cell line expressing GFP-LC3, the marker-protein for autophagosomes. Using stringent validation criteria, our screen identified nine novel autophagy regulators. Among the hits required for autophagosome formation are SCOC (short coiled-coil protein), a Golgi protein, which interacts with fasciculation and elongation protein zeta 1 (FEZ1), an ULK1-binding protein. SCOC forms a starvation-sensitive trimeric complex with UVRAG (UV radiation resistance associated gene) and FEZ1 and may regulate ULK1 and Beclin 1 complex activities. A second candidate WAC is required for starvation-induced autophagy but also acts as a potential negative regulator of the ubiquitin-proteasome system. The identification of these novel regulatory proteins with diverse functions in autophagy contributes towards a fuller understanding of autophagosome formation. A genome-wide siRNA screen identifies autophagy regulators. The Golgi protein SCOC regulates the interaction between ULK1 kinase and the Beclin 1 complexes in a nutrient-dependent manner; WAC enhances starvation-induced autophagy, while inhibiting the ubiquitin-proteasome system. Autophagy is a catabolic process by which cytoplasmic components are sequestered and transported by autophagosomes to lysosomes for degradation, enabling recycling of these components and providing cells with amino acids during starvation. It is a highly regulated process and its deregulation contributes to multiple diseases. Despite its importance in cell homeostasis, autophagy is not fully understood. To find new proteins that modulate starvation-induced autophagy, we performed a genome-wide siRNA screen in a stable human cell line expressing GFP–LC3, the marker-protein for autophagosomes. Using stringent validation criteria, our screen identified nine novel autophagy regulators. Among the hits required for autophagosome formation are SCOC (short coiled-coil protein), a Golgi protein, which interacts with fasciculation and elongation protein zeta 1 (FEZ1), an ULK1-binding protein. SCOC forms a starvation-sensitive trimeric complex with UVRAG (UV radiation resistance associated gene) and FEZ1 and may regulate ULK1 and Beclin 1 complex activities. A second candidate WAC is required for starvation-induced autophagy but also acts as a potential negative regulator of the ubiquitin-proteasome system. The identification of these novel regulatory proteins with diverse functions in autophagy contributes towards a fuller understanding of autophagosome formation. |
| Author | Howell, Michael Alemu, Endalkachew A McKnight, Nicole C Johansen, Terje Tooze, Sharon A Saunders, Rebecca E Jefferies, Harold B J |
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| BackLink | https://www.ncbi.nlm.nih.gov/pubmed/22354037$$D View this record in MEDLINE/PubMed |
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| Copyright | European Molecular Biology Organization 2012 Copyright © 2012 European Molecular Biology Organization Copyright Nature Publishing Group Apr 18, 2012 Copyright © 2012, European Molecular Biology Organization 2012 European Molecular Biology Organization |
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| DOI | 10.1038/emboj.2012.36 |
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| Keywords | WAC UVRAG SCOC FEZ1 siGenome screen |
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| Notes | ark:/67375/WNG-NMNVG2GB-X istex:BDB2C9D42C20EE23364972171688033B7D28A667 ArticleID:EMBJ201236 Supplementary DataSupplementary Table 1Supplementary Table 3Supplementary Table 4Review Process File ObjectType-Article-2 SourceType-Scholarly Journals-1 ObjectType-Feature-1 content type line 14 ObjectType-Article-1 ObjectType-Feature-2 content type line 23 Present address: Department of Neurology, Friedman Brain Institute, Mount Sinai School of Medicine, New York, NY 10029, USA |
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| Snippet | Autophagy is a catabolic process by which cytoplasmic components are sequestered and transported by autophagosomes to lysosomes for degradation, enabling... A genome-wide siRNA screen identifies autophagy regulators. The Golgi protein SCOC regulates the interaction between ULK1 kinase and the Beclin 1 complexes in... |
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| SubjectTerms | Amino acids Amino Acids - metabolism Autophagy Carrier Proteins - antagonists & inhibitors Carrier Proteins - metabolism Cell Line Deregulation EMBO07 EMBO20 FEZ1 Gene expression Gene Silencing Genes, Reporter Genomics Green Fluorescent Proteins - genetics Green Fluorescent Proteins - metabolism Humans Membrane Proteins - antagonists & inhibitors Membrane Proteins - metabolism Molecular biology Nuclear Proteins - antagonists & inhibitors Nuclear Proteins - metabolism Phagosomes - metabolism Proteins Recombinant Fusion Proteins - genetics Recombinant Fusion Proteins - metabolism Ribonucleic acid RNA RNA, Small Interfering - metabolism RNA-Binding Proteins SCOC siGenome screen Staining and Labeling Ultraviolet radiation UVRAG WAC |
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| Title | Genome-wide siRNA screen reveals amino acid starvation-induced autophagy requires SCOC and WAC |
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