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The COP1 E3-ligase interacts with FIP200, a key regulator of mammalian autophagy
BACKGROUND: The ubiquitin ligase COP1, COnstitutively Photomorphogenic 1, functions in many biological responses in mammalian cells, but its downstream pathway remains unclear. RESULTS: Here, we identified FIP200, a key regulator of mammalian autophagy, as a novel COP1-interacting protein by yeast t...
Autores principales: | , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
BioMed Central
2013
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3548756/ https://www.ncbi.nlm.nih.gov/pubmed/23289756 http://dx.doi.org/10.1186/1471-2091-14-1 |
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author | Kobayashi, Saori Yoneda-Kato, Noriko Itahara, Nagisa Yoshida, Akihiro Kato, Jun-ya |
author_facet | Kobayashi, Saori Yoneda-Kato, Noriko Itahara, Nagisa Yoshida, Akihiro Kato, Jun-ya |
author_sort | Kobayashi, Saori |
collection | PubMed |
description | BACKGROUND: The ubiquitin ligase COP1, COnstitutively Photomorphogenic 1, functions in many biological responses in mammalian cells, but its downstream pathway remains unclear. RESULTS: Here, we identified FIP200, a key regulator of mammalian autophagy, as a novel COP1-interacting protein by yeast two-hybrid screening. The interaction was confirmed by a GST-pulldown assay. Split-GFP analysis revealed that interaction between COP1 and FIP200 predominantly occurred in the cytoplasm and was enhanced in cells treated with UV irradiation. Different forms of FIP200 protein were expressed in cultured mammalian cells, and ectopic expression of COP1 reduced one of such forms. CONCLUSIONS: These data suggest that COP1 modulates FIP200-associated activities, which may contribute to a variety of cellular functions that COP1 is involved in. |
format | Online Article Text |
id | pubmed-3548756 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2013 |
publisher | BioMed Central |
record_format | MEDLINE/PubMed |
spelling | pubmed-35487562013-02-04 The COP1 E3-ligase interacts with FIP200, a key regulator of mammalian autophagy Kobayashi, Saori Yoneda-Kato, Noriko Itahara, Nagisa Yoshida, Akihiro Kato, Jun-ya BMC Biochem Research Article BACKGROUND: The ubiquitin ligase COP1, COnstitutively Photomorphogenic 1, functions in many biological responses in mammalian cells, but its downstream pathway remains unclear. RESULTS: Here, we identified FIP200, a key regulator of mammalian autophagy, as a novel COP1-interacting protein by yeast two-hybrid screening. The interaction was confirmed by a GST-pulldown assay. Split-GFP analysis revealed that interaction between COP1 and FIP200 predominantly occurred in the cytoplasm and was enhanced in cells treated with UV irradiation. Different forms of FIP200 protein were expressed in cultured mammalian cells, and ectopic expression of COP1 reduced one of such forms. CONCLUSIONS: These data suggest that COP1 modulates FIP200-associated activities, which may contribute to a variety of cellular functions that COP1 is involved in. BioMed Central 2013-01-06 /pmc/articles/PMC3548756/ /pubmed/23289756 http://dx.doi.org/10.1186/1471-2091-14-1 Text en Copyright ©2013 Kobayashi et al.; licensee BioMed Central Ltd. http://creativecommons.org/licenses/by/2.0 This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/2.0), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. |
spellingShingle | Research Article Kobayashi, Saori Yoneda-Kato, Noriko Itahara, Nagisa Yoshida, Akihiro Kato, Jun-ya The COP1 E3-ligase interacts with FIP200, a key regulator of mammalian autophagy |
title | The COP1 E3-ligase interacts with FIP200, a key regulator of mammalian autophagy |
title_full | The COP1 E3-ligase interacts with FIP200, a key regulator of mammalian autophagy |
title_fullStr | The COP1 E3-ligase interacts with FIP200, a key regulator of mammalian autophagy |
title_full_unstemmed | The COP1 E3-ligase interacts with FIP200, a key regulator of mammalian autophagy |
title_short | The COP1 E3-ligase interacts with FIP200, a key regulator of mammalian autophagy |
title_sort | cop1 e3-ligase interacts with fip200, a key regulator of mammalian autophagy |
topic | Research Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3548756/ https://www.ncbi.nlm.nih.gov/pubmed/23289756 http://dx.doi.org/10.1186/1471-2091-14-1 |
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