Phosphorylation-independent interaction between 14-3-3 protein and the plant plasma membrane H+-ATPase.
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.
Department of Plant Biology, Plant Physiology and Anatomy Laboratory, Royal Veterinary and Agricultural University, Thorvaldsensvej 40, 1871-Frederiksberg C, Copenhagen, Denmark.
J
J
Borch
K
K
Bych
P
P
Roepstorff
M G
MG
Palmgren
A T
AT
Fuglsang
D048948:14-3-3 Proteins; D000595:Amino Acid Sequence; D001665:Binding Sites; D002462:Cell Membrane / Q000201:enzymology; D008969:Molecular Sequence Data; D010446:Peptide Fragments / Q000737:chemistry; D010766:Phosphorylation; D010944:Plants / Q000201:enzymology*; D006180:Proton-Translocating ATPases / Q000737:chemistry / Q000378:metabolism*; D012441:Saccharomyces cerevisiae / Q000201:enzymology; D016415:Sequence Alignment; D017386:Sequence Homology, Amino Acid; D014446:Tyrosine 3-Monooxygenase / Q000737:chemistry / Q000378:metabolism*
D048948:14-3-3 Proteins; D010446:Peptide Fragments; D014446:Tyrosine 3-Monooxygenase; D006180:Proton-Translocating ATPases