dc.contributor.author | Daniel, K | |
dc.contributor.author | Icha, J | |
dc.contributor.author | Horenburg, C | |
dc.contributor.author | Müller, D | |
dc.contributor.author | Norden, C | |
dc.contributor.author | Mansfeld, J | |
dc.date.accessioned | 2020-08-26T13:24:44Z | |
dc.date.issued | 2018-08-17 | |
dc.identifier.citation | Nature communications, 2018, 9 (1), pp. 3297 - ? | |
dc.identifier.issn | 2041-1723 | |
dc.identifier.uri | https://repository.icr.ac.uk/handle/internal/4014 | |
dc.identifier.eissn | 2041-1723 | |
dc.identifier.doi | 10.1038/s41467-018-05855-5 | |
dc.description.abstract | The conditional and reversible depletion of proteins by auxin-mediated degradation is a powerful tool to investigate protein functions in cells and whole organisms. However, its wider applications require fusing the auxin-inducible degron (AID) to individual target proteins. Thus, establishing the auxin system for multiple proteins can be challenging. Another approach for directed protein degradation are anti-GFP nanobodies, which can be applied to GFP stock collections that are readily available in different experimental models. Here, we combine the advantages of auxin and nanobody-based degradation technologies creating an AID-nanobody to degrade GFP-tagged proteins at different cellular structures in a conditional and reversible manner in human cells. We demonstrate efficient and reversible inactivation of the anaphase promoting complex/cyclosome (APC/C) and thus provide new means to study the functions of this essential ubiquitin E3 ligase. Further, we establish auxin degradation in a vertebrate model organism by employing AID-nanobodies in zebrafish. | |
dc.format | Electronic | |
dc.format.extent | 3297 - ? | |
dc.language | eng | |
dc.language.iso | eng | |
dc.publisher | NATURE PUBLISHING GROUP | |
dc.rights.uri | https://creativecommons.org/licenses/by/4.0 | |
dc.subject | Hela Cells | |
dc.subject | Animals | |
dc.subject | Zebrafish | |
dc.subject | Humans | |
dc.subject | Indoleacetic Acids | |
dc.subject | Lysine | |
dc.subject | Green Fluorescent Proteins | |
dc.subject | Recombinant Fusion Proteins | |
dc.subject | Cell Compartmentation | |
dc.subject | Kinetics | |
dc.subject | Proteolysis | |
dc.subject | Single-Domain Antibodies | |
dc.subject | Anaphase-Promoting Complex-Cyclosome | |
dc.title | Conditional control of fluorescent protein degradation by an auxin-dependent nanobody. | |
dc.type | Journal Article | |
dcterms.dateAccepted | 2018-07-27 | |
rioxxterms.versionofrecord | 10.1038/s41467-018-05855-5 | |
rioxxterms.licenseref.uri | https://creativecommons.org/licenses/by/4.0 | |
rioxxterms.licenseref.startdate | 2018-08-17 | |
rioxxterms.type | Journal Article/Review | |
dc.relation.isPartOf | Nature communications | |
pubs.issue | 1 | |
pubs.notes | No embargo | |
pubs.organisational-group | /ICR | |
pubs.organisational-group | /ICR/Primary Group | |
pubs.organisational-group | /ICR/Primary Group/ICR Divisions | |
pubs.organisational-group | /ICR/Primary Group/ICR Divisions/Cancer Biology | |
pubs.organisational-group | /ICR/Primary Group/ICR Divisions/Cancer Biology/Post-translational modifications and cell proliferation | |
pubs.organisational-group | /ICR | |
pubs.organisational-group | /ICR/Primary Group | |
pubs.organisational-group | /ICR/Primary Group/ICR Divisions | |
pubs.organisational-group | /ICR/Primary Group/ICR Divisions/Cancer Biology | |
pubs.organisational-group | /ICR/Primary Group/ICR Divisions/Cancer Biology/Post-translational modifications and cell proliferation | |
pubs.publication-status | Published | |
pubs.volume | 9 | |
pubs.embargo.terms | No embargo | |
icr.researchteam | Post-translational modifications and cell proliferation | |
dc.contributor.icrauthor | Mansfeld, Joerg | |