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An optimized optogenetic clustering tool for probing protein interaction and function

Author

Listed:
  • Amir Taslimi

    (University of Colorado School of Medicine)

  • Justin D. Vrana

    (University of Colorado School of Medicine)

  • Daniel Chen

    (University of Colorado School of Medicine)

  • Sofya Borinskaya

    (Raymond and Beverly Sackler Laboratory of Genetics and Molecular Medicine, University of Connecticut Health Center)

  • Bruce J. Mayer

    (Raymond and Beverly Sackler Laboratory of Genetics and Molecular Medicine, University of Connecticut Health Center)

  • Matthew J. Kennedy

    (University of Colorado School of Medicine)

  • Chandra L. Tucker

    (University of Colorado School of Medicine)

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.

Suggested Citation

  • Amir Taslimi & Justin D. Vrana & Daniel Chen & Sofya Borinskaya & Bruce J. Mayer & Matthew J. Kennedy & Chandra L. Tucker, 2014. "An optimized optogenetic clustering tool for probing protein interaction and function," Nature Communications, Nature, vol. 5(1), pages 1-9, December.
    • Handle: RePEc:nat:natcom:v:5:y:2014:i:1:d:10.1038_ncomms5925
    DOI: 10.1038/ncomms5925
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    Cited by:

    1. Harpreet Kaur Salgania & Jutta Metz & Mandy Jeske, 2024. "ReLo is a simple and rapid colocalization assay to identify and characterize direct protein–protein interactions," Nature Communications, Nature, vol. 15(1), pages 1-12, December.
    2. Dennis Vettkötter & Martin Schneider & Brady D. Goulden & Holger Dill & Jana Liewald & Sandra Zeiler & Julia Guldan & Yilmaz Arda Ateş & Shigeki Watanabe & Alexander Gottschalk, 2022. "Rapid and reversible optogenetic silencing of synaptic transmission by clustering of synaptic vesicles," Nature Communications, Nature, vol. 13(1), pages 1-17, December.
    3. Liyuan Zhu & Harold M. McNamara & Jared E. Toettcher, 2023. "Light-switchable transcription factors obtained by direct screening in mammalian cells," Nature Communications, Nature, vol. 14(1), pages 1-16, December.
    4. Yaling Dou & Rui Chen & Siyao Liu & Yi-Tsang Lee & Ji Jing & Xiaoxuan Liu & Yuepeng Ke & Rui Wang & Yubin Zhou & Yun Huang, 2023. "Optogenetic engineering of STING signaling allows remote immunomodulation to enhance cancer immunotherapy," Nature Communications, Nature, vol. 14(1), pages 1-17, December.
    5. Charlotte A. Cialek & Gabriel Galindo & Tatsuya Morisaki & Ning Zhao & Taiowa A. Montgomery & Timothy J. Stasevich, 2022. "Imaging translational control by Argonaute with single-molecule resolution in live cells," Nature Communications, Nature, vol. 13(1), pages 1-14, December.

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