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Biochemical analysis of the transducin-phosphodiesterase interaction

Nature Structural Biology volume 1, pages 771–781 (1994)Cite this article

Abstract

In vertebrate rod cells, the activated α-subunit of rod transducin interacts with the γ (regulatory) subunits of phosphodiesterase to disinhibit the catalytic subunits. A 22-amino acid long region of rod transducin involved in phosphodiesterase activation has recently been identified. We have used peptides from this region of rod transducin and from several other G protein α-subunits to study the nature and specificity of the G protein α-effector interaction. Although peptides derived from rod transducin, cone transducin and gustducin are similar, only the rod peptide is capable of activating rod phosphodiesterase. Using substituted peptides we have identified five residues on one exposed face of rod transducin as important to phosphodiesterase activation. These results disagree with previous models which propose that loop regions of rod transducin interact with phosphodiesterase γ

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Author notes

  1. Alain Robichon

    Present address: New York University, New York, NY, USA

Authors and Affiliations

  1. Roche Institute of Molecular Biology, NJ, 07110, USA

    Nancy Spickofsky, Alain Robichon & Robert F. Margolskee

  2. Roche Research Center, Nutley, NJ, 07110, USA

    Nancy Spickofsky, Alain Robichon, Waleed Danho, David Fry, David Greeley, Bradford Graves, Vincent Madison & Robert F. Margolskee

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  1. Nancy Spickofsky
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Spickofsky, N., Robichon, A., Danho, W. et al. Biochemical analysis of the transducin-phosphodiesterase interaction. Nat Struct Mol Biol 1, 771–781 (1994). https://doi.org/10.1038/nsb1194-771

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