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An optimized optogenetic clustering tool for probing protein interaction and function
Open accessAbstract
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. Protein–protein interactions are fundamental to nearly all molecular and cellular processes. Here Taslimi et al.describe a versatile new optogenetic module that can be used to visualize protein–protein interactions, as well as reversibly control them with light with spatiotemporal resolution.
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Metadata
- Authors
- Taslimi, A., Vrana, J. D., Chen, D., Borinskaya, S., Mayer, B. J., Kennedy, M. J., & Tucker, C. L.
- Venue
- Nature Communications
- Published
- 2014-09-18
- Volume
- 5
- Issue
- 1
- Pages
- 4925-4925
- ISSN
- 2041-1723 (ISSN-L)
- OpenAlex
- W2055045552
- Cited by
- 386
- References
- 44
- FWCI
- 9.66
- Type
- journal article
- Language
- en
- Open access
- bronze
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