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Curated Optogenetic Publication Database

Search precisely and efficiently by using the advantage of the hand-assigned publication tags that allow you to search for papers involving a specific trait, e.g. a particular optogenetic switch or a host organism.

Qr: switch:"CRY2olig"
Showing 126 - 128 of 128 results
126.

Optimizing optogenetic constructs for control over signaling and cell behaviours.

blue red BLUF domains Cryptochromes LOV domains Phytochromes Review
Photochem Photobiol Sci, 2 Jul 2015 DOI: 10.1039/c5pp00171d Link to full text
Abstract: Optogenetic tools have recently been developed that enable dynamic control over the activities of select signaling proteins. They provide the unique ability to rapidly turn signaling events on or off with subcellular control in living cells and organisms. This capability is leading to new insights into how the spatial and temporal coordination of signaling events governs dynamic cell behaviours such as migration and neurite outgrowth. These tools can also be used to dissect a protein's signaling functions at different organelles. Here we review the properties of photoreceptors from diverse organisms that have been leveraged to control signaling in mammalian cells. We emphasize recent engineering approaches that have been used to create optogenetic constructs with optimized spectral, kinetic, and signaling properties for controlling cell behaviours.
127.

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

blue CRY2/CRY2 CRY2olig Cos-7 HEK293 S. cerevisiae Control of cytoskeleton / cell motility / cell shape Control of intracellular / vesicular transport
Nat Commun, 18 Sep 2014 DOI: 10.1038/ncomms5925 Link to full text
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.
128.

A comparison of the substrate specificities of endo-beta-N-acetylglucosaminidases from Streptomyces griseus and Diplococcus Pneumoniae.

blue BLUF domains Cryptochromes LOV domains CHO DP-12 Background
Biochem Biophys Res Commun, 3 Nov 1975 DOI: 10.1007/s00253-024-13363-4 Link to full text
Abstract: Abstract not available.
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