14-3-3 Protein homologues play a central role in the fusicoccin signal transduction pathway |
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Authors: | Albertus H. De Boer Henrie A. A. J. Korthout |
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Affiliation: | (1) Department of Plant Physiology and Biochemistry, Institute of Molecular Biological Sciences, Vrije Universiteit, De Boelelaan 1087, 1081 HV Amsterdam, The Netherlands |
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Abstract: | The plasma membrane located fusicoccin binding protein (FCBP) is an essential element in the fusicoccin (FC) signal transduction pathway. We obtained primary sequence information for the 31 kD subunit of the FCBP. These sequences showed that the FCBP is homologous to members of the 14-3-3 protein family. Both the 31 and 30 kD subunits cross-react with 14-3-3 antibodies. In native form the FCBP occurs as a dimer, but it is also part of a complex with higher molecular mass. The monomeric forms of the FCBP (the 30 and 31 kD subunits) do not have 3H-FC binding activity. We discuss how the FCBP, as a member of the 14-3-3 protein family, may be able to bind FC and how the FC-signal is transduced to the effector protein, the H+-ATPase. |
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Keywords: | Avena sativa fusicoccin receptor 14-3-3 proteins kinase plasma membrane |
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