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Determination of the Photoisomerization Quantum Yield of a Hydrazone Photoswitch
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Optimizing photoswitchable MEK.

Aleena L Patel1,2,3, Eyan Yeung2,3, Sarah E McGuire1

  • 1Department of Chemical and Biological Engineering, Princeton University, Princeton, NJ 08544.

Proceedings of the National Academy of Sciences of the United States of America
|December 5, 2019
PubMed
Summary
This summary is machine-generated.

Optimized optogenetic tools enhance studies of cell signaling. Modified photoswitchable MEK1 (psMEK) enzymes regain maximal activity, enabling precise control over ERK signaling in vivo.

Keywords:
ERK signalingoptogeneticsphotoswitchable MEK

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Area of Science:

  • Molecular Biology
  • Cell Signaling
  • Optogenetics

Background:

  • Optogenetics offers new ways to study cell signaling quantitatively.
  • A photoswitchable MEK1 (psMEK) enzyme was developed to control the ERK pathway.
  • psMEK's catalytic activity is limited due to phosphorylation-mimicking mutations.

Purpose of the Study:

  • To address the suboptimal functionality of psMEK in vivo.
  • To enhance psMEK's catalytic activity while maintaining optogenetic control.
  • To enable new quantitative studies of ERK signaling dynamics.

Main Methods:

  • Engineered psMEK by combining phosphomimetic mutations with gain-of-function, destabilizing mutations.
  • Assessed kinase activity in vitro and in vivo in Drosophila and zebrafish.
  • Used optimized psMEK to deliver controlled ERK activation pulses during zebrafish embryogenesis.

Main Results:

  • Combining mutations restored maximal kinase activity in vitro.
  • The engineered psMEK retained reversible activation in vivo.
  • ERK activation pulses revealed rheostat-like responses in a morphogenetic event.

Conclusions:

  • Optimized psMEK overcomes limitations of previous optogenetic tools.
  • This enhanced tool allows precise temporal control of ERK signaling.
  • The approach facilitates quantitative analysis of signaling-dependent biological processes.