dc.contributor.author
An, Wenlin
dc.contributor.author
Jackson, Rachel E.
dc.contributor.author
Hunter, Paul
dc.contributor.author
Gögel, Stefanie
dc.contributor.author
Diepen, Michiel van
dc.contributor.author
Liu, Karen
dc.contributor.author
Meyer, Martin P.
dc.contributor.author
Eickholt, Britta J.
dc.date.accessioned
2018-06-08T03:30:36Z
dc.date.available
2016-02-04T11:31:28.521Z
dc.identifier.uri
https://refubium.fu-berlin.de/handle/fub188/15331
dc.identifier.uri
http://dx.doi.org/10.17169/refubium-19519
dc.description.abstract
Targeting protein stability with small molecules has emerged as an effective
tool to control protein abundance in a fast, scalable and reversible manner.
The technique involves tagging a protein of interest (POI) with a
destabilizing domain (DD) specifically controlled by a small molecule. The
successful construction of such fusion proteins may, however, be limited by
functional interference of the DD epitope with electrostatic interactions
required for full biological function of proteins. Another drawback of this
approach is the remaining endogenous protein. Here, we combined the Cre-LoxP
system with an advanced DD and generated a protein regulation system in which
the loss of an endogenous protein, in our case the tumor suppressor PTEN, can
be coupled directly with a conditionally fine-tunable DD-PTEN. This new system
will consolidate and extend the use of DD-technology to control protein
function precisely in living cells and animal models.
en
dc.rights.uri
http://creativecommons.org/licenses/by/4.0/
dc.subject.ddc
600 Technik, Medizin, angewandte Wissenschaften::610 Medizin und Gesundheit
dc.title
Engineering FKBP-Based Destabilizing Domains to Build Sophisticated Protein
Regulation Systems
dc.type
Wissenschaftlicher Artikel
dcterms.bibliographicCitation
PLoS ONE. - 10 (2015), 12, Artikel Nr. e0145783
dcterms.bibliographicCitation.doi
10.1371/journal.pone.0145783
dcterms.bibliographicCitation.url
http://journals.plos.org/plosone/article?id=10.1371/journal.pone.0145783
refubium.affiliation
Charité - Universitätsmedizin Berlin
de
refubium.mycore.fudocsId
FUDOCS_document_000000023849
refubium.note.author
Der Artikel wurde in einer Open-Access-Zeitschrift publiziert.
refubium.resourceType.isindependentpub
no
refubium.mycore.derivateId
FUDOCS_derivate_000000005948
dcterms.accessRights.openaire
open access