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A multivalent PDZ-domain protein assembles signalling complexes in a G-protein-coupled cascade

Author

Listed:
  • Susan Tsunoda

    (University of California at San Diego)

  • Jimena Sierralta

    (University of California at San Diego)

  • Yumei Sun

    (University of California at San Diego)

  • Ruth Bodner

    (University of California at San Diego)

  • Emiko Suzuki

    (*The Insitute of Medical Science, The University of Tokyo)

  • Ann Becker

    (University of California at San Diego)

  • Michael Socolich

    (University of California at San Diego)

  • Charles S. Zuker

    (University of California at San Diego)

Abstract

How are signalling molecules organized into different pathways within the same cell? In Drosophila, the inaD gene encodes a protein consisting of five PDZ domains which serves as a scaffold to assemble different components of the phototransduction cascade, including the principal light-activated ion channels, the effector phospholipase C-β and protein kinase C. Null inaD mutants have a dramatically reorganized subcellular distribution of signalling molecules, and a total loss of transduction complexes. Also, mutants defective in a single PDZ domain produce signalling complexes that lack the target protein and display corresponding defects in their physiology. A picture emerges of a highly organized unit of signalling, a ‘transducisome’, with PDZ domains functioning as key elements in the organization of transduction complexes in vivo.

Suggested Citation

  • Susan Tsunoda & Jimena Sierralta & Yumei Sun & Ruth Bodner & Emiko Suzuki & Ann Becker & Michael Socolich & Charles S. Zuker, 1997. "A multivalent PDZ-domain protein assembles signalling complexes in a G-protein-coupled cascade," Nature, Nature, vol. 388(6639), pages 243-249, July.
  • Handle: RePEc:nat:nature:v:388:y:1997:i:6639:d:10.1038_40805
    DOI: 10.1038/40805
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    Cited by:

    1. Khaled Daqrouq & Rami Alhmouz & Ahmed Balamesh & Adnan Memic, 2015. "Application of Wavelet Transform for PDZ Domain Classification," PLOS ONE, Public Library of Science, vol. 10(4), pages 1-16, April.

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