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Chemical development of intracellular protein heterodimerizers

Erhart, D. and Zimmermann, M. and Jacques, O. and Wittwer, M. B. and Ernst, B. and Constable, E. and Zvelebil, M. and Beaufils, F. and Wymann, M. P.. (2013) Chemical development of intracellular protein heterodimerizers. Chemistry & Biology, 20 (4). pp. 549-557.

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Official URL: http://edoc.unibas.ch/dok/A6211898

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Abstract

Cell activation initiated by receptor ligands or oncogenes triggers complex and convoluted intracellular signaling. Techniques initiating signals at defined starting points and cellular locations are attractive to elucidate the output of selected pathways. Here, we present the development and validation of a protein heterodimerization system based on small molecules cross-linking fusion proteins derived from HaloTags and SNAP-tags. Chemical dimerizers of HaloTag and SNAP-tag (HaXS) show excellent selectivity and have been optimized for intracellular reactivity. HaXS force protein-protein interactions and can translocate proteins to various cellular compartments. Due to the covalent nature of the HaloTag-HaXS-SNAP-tag complex, intracellular dimerization can be easily monitored. First applications include protein targeting to cytoskeleton, to the plasma membrane, to lysosomes, the initiation of the PI3K/mTOR pathway, and multiplexed protein complex formation in combination with the rapamycin dimerization system.
Faculties and Departments:03 Faculty of Medicine > Departement Biomedizin > Division of Biochemistry and Genetics > Cancer- and Immunobiology (Wymann)
05 Faculty of Science > Departement Pharmazeutische Wissenschaften > Pharmazie > Molekulare Pharmazie (Ernst)
UniBasel Contributors:Ernst, Beat and Wymann, Matthias P.
Item Type:Article, refereed
Article Subtype:Research Article
Bibsysno:Link to catalogue
Publisher:Cell Press
ISSN:1074-5521
Note:Publication type according to Uni Basel Research Database: Journal article
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Last Modified:28 Nov 2017 11:08
Deposited On:31 Jan 2014 09:49

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