An optimized optogenetic clustering tool for probing protein interaction and function

Amir Taslimi, Justin D. Vrana, Daniel Chen, Sofya Borinskaya, Bruce J. Mayer, Matthew J. Kennedy and Chandra L. Tucker ()
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Amir Taslimi: University of Colorado School of Medicine
Justin D. Vrana: University of Colorado School of Medicine
Daniel Chen: University of Colorado School of Medicine
Sofya Borinskaya: Raymond and Beverly Sackler Laboratory of Genetics and Molecular Medicine, University of Connecticut Health Center
Bruce J. Mayer: Raymond and Beverly Sackler Laboratory of Genetics and Molecular Medicine, University of Connecticut Health Center
Matthew J. Kennedy: University of Colorado School of Medicine
Chandra L. Tucker: University of Colorado School of Medicine

Nature Communications, 2014, vol. 5, issue 1, 1-9

Abstract: 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.

Date: 2014
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DOI: 10.1038/ncomms5925

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