The dark side of EGFP: defective polyubiquitination.
Enhanced Green Fluorescent Protein (EGFP) is the most commonly used live cell reporter despite a number of conflicting reports that it can affect cell physiology. Thus far, the precise mechanism of GFP-associated defects remained unclear. Here we demonstrate that EGFP and EGFP fusion proteins inhibi...
| Main Authors: | , , , , , , , |
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| Format: | Article |
| Language: | English |
| Published: |
Public Library of Science (PLoS)
2006-01-01
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| Series: | PLoS ONE |
| Online Access: | http://europepmc.org/articles/PMC1762387?pdf=render |
| _version_ | 1818014585597198336 |
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| author | Mathijs Baens Heidi Noels Vicky Broeckx Sofie Hagens Sabine Fevery An D Billiau Hugo Vankelecom Peter Marynen |
| author_facet | Mathijs Baens Heidi Noels Vicky Broeckx Sofie Hagens Sabine Fevery An D Billiau Hugo Vankelecom Peter Marynen |
| author_sort | Mathijs Baens |
| collection | DOAJ |
| description | Enhanced Green Fluorescent Protein (EGFP) is the most commonly used live cell reporter despite a number of conflicting reports that it can affect cell physiology. Thus far, the precise mechanism of GFP-associated defects remained unclear. Here we demonstrate that EGFP and EGFP fusion proteins inhibit polyubiquitination, a posttranslational modification that controls a wide variety of cellular processes, like activation of kinase signalling or protein degradation by the proteasome. As a consequence, the NF-kappaB and JNK signalling pathways are less responsive to activation, and the stability of the p53 tumour suppressor is enhanced in cell lines and in vivo. In view of the emerging role of polyubiquitination in the regulation of numerous cellular processes, the use of EGFP as a live cell reporter should be carefully considered. |
| first_indexed | 2024-04-14T06:47:21Z |
| format | Article |
| id | doaj.art-23c6ea4d94794086be9039095d81aa4d |
| institution | Directory Open Access Journal |
| issn | 1932-6203 |
| language | English |
| last_indexed | 2024-04-14T06:47:21Z |
| publishDate | 2006-01-01 |
| publisher | Public Library of Science (PLoS) |
| record_format | Article |
| series | PLoS ONE |
| spelling | doaj.art-23c6ea4d94794086be9039095d81aa4d2022-12-22T02:07:08ZengPublic Library of Science (PLoS)PLoS ONE1932-62032006-01-011e5410.1371/journal.pone.0000054The dark side of EGFP: defective polyubiquitination.Mathijs BaensHeidi NoelsVicky BroeckxSofie HagensSabine FeveryAn D BilliauHugo VankelecomPeter MarynenEnhanced Green Fluorescent Protein (EGFP) is the most commonly used live cell reporter despite a number of conflicting reports that it can affect cell physiology. Thus far, the precise mechanism of GFP-associated defects remained unclear. Here we demonstrate that EGFP and EGFP fusion proteins inhibit polyubiquitination, a posttranslational modification that controls a wide variety of cellular processes, like activation of kinase signalling or protein degradation by the proteasome. As a consequence, the NF-kappaB and JNK signalling pathways are less responsive to activation, and the stability of the p53 tumour suppressor is enhanced in cell lines and in vivo. In view of the emerging role of polyubiquitination in the regulation of numerous cellular processes, the use of EGFP as a live cell reporter should be carefully considered.http://europepmc.org/articles/PMC1762387?pdf=render |
| spellingShingle | Mathijs Baens Heidi Noels Vicky Broeckx Sofie Hagens Sabine Fevery An D Billiau Hugo Vankelecom Peter Marynen The dark side of EGFP: defective polyubiquitination. PLoS ONE |
| title | The dark side of EGFP: defective polyubiquitination. |
| title_full | The dark side of EGFP: defective polyubiquitination. |
| title_fullStr | The dark side of EGFP: defective polyubiquitination. |
| title_full_unstemmed | The dark side of EGFP: defective polyubiquitination. |
| title_short | The dark side of EGFP: defective polyubiquitination. |
| title_sort | dark side of egfp defective polyubiquitination |
| url | http://europepmc.org/articles/PMC1762387?pdf=render |
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