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Nat Commun. 2014 Sep 18;5:4925. doi: 10.1038/ncomms5925.

An optimized optogenetic clustering tool for probing protein interaction and function.

Author information

  • 1Department of Pharmacology, University of Colorado School of Medicine, Aurora, Colorado 80045, USA.
  • 2Raymond and Beverly Sackler Laboratory of Genetics and Molecular Medicine, Department of Genetics and Molecular Biology, University of Connecticut Health Center, Farmington, Connecticut 06030, USA.

Abstract

The Arabidopsis photoreceptor cryptochrome 2 (CRY2) was previously used as an optogenetic module, allowing spatiotemporal control of cellular processes with light. Here we report the development of a new CRY2-derived optogenetic module, 'CRY2olig', which induces rapid, robust, and reversible protein oligomerization in response to light. Using this module, we developed a novel protein interaction assay, Light-Induced Co-clustering, that can be used to interrogate protein interaction dynamics in live cells. In addition to use probing protein interactions, CRY2olig can also be used to induce and reversibly control diverse cellular processes with spatial and temporal resolution. Here we demonstrate disrupting clathrin-mediated endocytosis and promoting Arp2/3-mediated actin polymerization with light. These new CRY2-based approaches expand the growing arsenal of optogenetic strategies to probe cellular function.

PMID:
25233328
PMCID:
PMC4170572
DOI:
10.1038/ncomms5925
[PubMed - indexed for MEDLINE]
Free PMC Article
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