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Spatiotemporal control of cell signalling using a light-switchable protein interaction

Author

Listed:
  • Anselm Levskaya

    (The Cell Propulsion Lab, UCSF/UCB NIH Nanomedicine Development Center,
    Graduate Program in Biophysics,
    Department of Pharmaceutical Chemistry,)

  • Orion D. Weiner

    (The Cell Propulsion Lab, UCSF/UCB NIH Nanomedicine Development Center,
    Cardiovascular Research Institute,)

  • Wendell A. Lim

    (The Cell Propulsion Lab, UCSF/UCB NIH Nanomedicine Development Center,
    University of California, San Francisco, California 94158-2517, USA)

  • Christopher A. Voigt

    (The Cell Propulsion Lab, UCSF/UCB NIH Nanomedicine Development Center,
    Department of Pharmaceutical Chemistry,)

Abstract

Cell biology's leading lights Green fluorescent protein and other genetically encodable optical reporters have revolutionized the study of cell function. Now Levskaya et al. describe a technology that adds a new dimension to cell biology by incorporating light-activated proteins from plants into mammalian cell signalling systems, leading to cells whose morphology and behaviour can be controlled by light. The system uses a reversible protein–protein interaction module from the Arabidopsis phytochrome-signalling network to reversibly translocate activators of the Rho-family GTPases to the plasma membrane. In principle, this advance makes it possible to design a variety of light-programmable reagents for a new generation of perturbative cell biology experiments.

Suggested Citation

  • Anselm Levskaya & Orion D. Weiner & Wendell A. Lim & Christopher A. Voigt, 2009. "Spatiotemporal control of cell signalling using a light-switchable protein interaction," Nature, Nature, vol. 461(7266), pages 997-1001, October.
  • Handle: RePEc:nat:nature:v:461:y:2009:i:7266:d:10.1038_nature08446
    DOI: 10.1038/nature08446
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    Cited by:

    1. Ellen H. Brumbaugh-Reed & Yang Gao & Kazuhiro Aoki & Jared E. Toettcher, 2024. "Rapid and reversible dissolution of biomolecular condensates using light-controlled recruitment of a solubility tag," Nature Communications, Nature, vol. 15(1), pages 1-13, December.
    2. Willow Coyote-Maestas & David Nedrud & Antonio Suma & Yungui He & Kenneth A. Matreyek & Douglas M. Fowler & Vincenzo Carnevale & Chad L. Myers & Daniel Schmidt, 2021. "Probing ion channel functional architecture and domain recombination compatibility by massively parallel domain insertion profiling," Nature Communications, Nature, vol. 12(1), pages 1-16, December.
    3. Kei Yamamoto & Haruko Miura & Motohiko Ishida & Yusuke Mii & Noriyuki Kinoshita & Shinji Takada & Naoto Ueno & Satoshi Sawai & Yohei Kondo & Kazuhiro Aoki, 2021. "Optogenetic relaxation of actomyosin contractility uncovers mechanistic roles of cortical tension during cytokinesis," Nature Communications, Nature, vol. 12(1), pages 1-13, December.
    4. Takayuki Yasunaga & Johannes Wiegel & Max D. Bergen & Martin Helmstädter & Daniel Epting & Andrea Paolini & Özgün Çiçek & Gerald Radziwill & Christina Engel & Thomas Brox & Olaf Ronneberger & Peter Wa, 2022. "Microridge-like structures anchor motile cilia," Nature Communications, Nature, vol. 13(1), pages 1-14, December.
    5. Judee A. Sharon & Chelsea Dasrath & Aiden Fujiwara & Alessandro Snyder & Mace Blank & Sam O’Brien & Lauren M. Aufdembrink & Aaron E. Engelhart & Katarzyna P. Adamala, 2023. "Trumpet is an operating system for simple and robust cell-free biocomputing," Nature Communications, Nature, vol. 14(1), pages 1-12, December.

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