Abstract
A common approach to isolate hormone receptors is the preparation of a protein fraction with high affinity to a particular hormone. The search for an auxin receptor can be traced back to 1972 when Hertel and his coworkers prepared a membrane fraction with auxin binding activity. In subsequent publications up to three kinetically distinguishable auxin binding sites have been described and thoroughly been characterized (Batt & Venis 1976, Batt et al 1976, Cross & Briggs 1978,1979, Dohrmann et al 1978, Löbler & Klämbt 1985a, Murphy 1980, Ray et al 1977 a/b, Shimomura et al 1986, Tappeser et al 1981, Venis 1977 a/b, 1980). However, the only criterion for an auxin receptor has been its high affinity for auxin, but the data for a signal transduction after auxin binding, leading to a physiological response, was lacking. Indirect evidence for a receptor function of the site I auxin binding was given by the modulation of the auxin binding capacity by light (Walton & Ray 1981). An inhibition of auxin Induced elongation growth by anti receptor antibodies clearly showed the involvement of the auxin receptor in signal transduction (Löbler & Klämbt 1985b).
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Literature
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Löbler, M., Klämbt, D. (1987). The Auxin Receptor in Corn Coleoptiles. In: Klämbt, D. (eds) Plant Hormone Receptors. NATO ASI Series, vol 10. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-72779-5_4
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DOI: https://doi.org/10.1007/978-3-642-72779-5_4
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