Citation

BibTex format

@article{Frank:2016:10.1038/nchembio.2141,
author = {Frank, JA and Yushchenko, DA and Hodson, DJ and Lipstein, N and Nagpal, J and Rutter, GA and Rhee, JS and Gottschalk, A and Brose, N and Schultz, C and Trauner, D},
doi = {10.1038/nchembio.2141},
journal = {Nature Chemical Biology},
pages = {755--762},
title = {Photoswitchable diacylglycerols enable optical control of protein kinase C.},
url = {http://dx.doi.org/10.1038/nchembio.2141},
volume = {12},
year = {2016}
}

RIS format (EndNote, RefMan)

TY  - JOUR
AB - Increased levels of the second messenger lipid diacylglycerol (DAG) induce downstream signaling events including the translocation of C1-domain-containing proteins toward the plasma membrane. Here, we introduce three light-sensitive DAGs, termed PhoDAGs, which feature a photoswitchable acyl chain. The PhoDAGs are inactive in the dark and promote the translocation of proteins that feature C1 domains toward the plasma membrane upon a flash of UV-A light. This effect is quickly reversed after the termination of photostimulation or by irradiation with blue light, permitting the generation of oscillation patterns. Both protein kinase C and Munc13 can thus be put under optical control. PhoDAGs control vesicle release in excitable cells, such as mouse pancreatic islets and hippocampal neurons, and modulate synaptic transmission in Caenorhabditis elegans. As such, the PhoDAGs afford an unprecedented degree of spatiotemporal control and are broadly applicable tools to study DAG signaling.
AU - Frank,JA
AU - Yushchenko,DA
AU - Hodson,DJ
AU - Lipstein,N
AU - Nagpal,J
AU - Rutter,GA
AU - Rhee,JS
AU - Gottschalk,A
AU - Brose,N
AU - Schultz,C
AU - Trauner,D
DO - 10.1038/nchembio.2141
EP - 762
PY - 2016///
SN - 1552-4469
SP - 755
TI - Photoswitchable diacylglycerols enable optical control of protein kinase C.
T2 - Nature Chemical Biology
UR - http://dx.doi.org/10.1038/nchembio.2141
UR - http://hdl.handle.net/10044/1/43691
VL - 12
ER -