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Localized light-induced protein dimerization in living cells using a photocaged dimerizer.


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.

SUBMITTER: Ballister ER 

PROVIDER: S-EPMC4308733 | biostudies-literature | 2014 Nov

REPOSITORIES: biostudies-literature

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Localized light-induced protein dimerization in living cells using a photocaged dimerizer.

Ballister Edward R ER   Aonbangkhen Chanat C   Mayo Alyssa M AM   Lampson Michael A MA   Chenoweth David M DM  

Nature communications 20141117


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  ...[more]

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