Phosphorylation-independent interaction between 14-3-3 protein and the plant plasma membrane H+-ATPase |
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Authors: | Borch J Bych K Roepstorff P Palmgren M G Fuglsang A T |
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Affiliation: | Department of Plant Biology, Plant Physiology and Anatomy Laboratory, Royal Veterinary and Agricultural University, Thorvaldsensvej 40, 1871-Frederiksberg C, Copenhagen, Denmark. |
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Abstract: | 14-3-3 proteins interact with a novel phosphothreonine motif (Y(946)pTV) at the extreme C-terminal end of the plant plasma membrane H(+)-ATPase molecule. Phosphorylation-independent binding of 14-3-3 protein to the YTV motif can be induced by the fungal phytotoxin fusicoccin. The molecular basis for the phosphorylation-independent interaction between 14-3-3 and H(+)-ATPase in the presence of fusicoccin has been investigated in more detail. Fusicoccin binds to a heteromeric receptor that involves both 14-3-3 protein and H(+)-ATPase. Binding of fusicoccin is dependent upon the YTV motif in the H(+)-ATPase and, in addition, requires residues further upstream of this motif. Apparently, 14-3-3 proteins interact with the unusual epitope in H(+)-ATPase via its conserved amphipathic groove. This implies that very diverse epitopes bind to a common structure in the 14-3-3 protein. |
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