| Literature DB >> 25400104 |
Edward R Ballister1, Chanat Aonbangkhen2, Alyssa M Mayo1, Michael A Lampson1, David M Chenoweth2.
Abstract
Regulated protein localization is critical for many cellular processes. Several techniques have been developed for experimental control over protein localization, including chemically induced and light-induced dimerization, which both provide temporal control. Light-induced dimerization offers the distinct advantage of spatial precision within subcellular length scales. A number of elegant systems have been reported that utilize natural light-sensitive proteins to induce dimerization via direct protein-protein binding interactions, but the application of these systems at cellular locations beyond the plasma membrane has been limited. Here we present a new technique to rapidly and reversibly control protein localization in living cells with subcellular spatial resolution using a cell-permeable, photoactivatable chemical inducer of dimerization. We demonstrate light-induced recruitment of a cytosolic protein to individual centromeres, kinetochores, mitochondria and centrosomes in human cells, indicating that our system is widely applicable to many cellular locations.Entities:
Mesh:
Substances:
Year: 2014 PMID: 25400104 PMCID: PMC4308733 DOI: 10.1038/ncomms6475
Source DB: PubMed Journal: Nat Commun ISSN: 2041-1723 Impact factor: 14.919