title: Binding of 14-3-3 protein to the plasma membrane H(+)-ATPase AHA2 involves the three C-terminal residues Tyr(946)-Thr-Val and requires phosphorylation of Thr(947).
abstract: 14-3-3 proteins play a regulatory role in a diverse array of cellular functions such as apoptosis, regulation of the cell cycle, and regulation of gene transcription. The phytotoxin fusicoccin specifically induces association of virtually any 14-3-3 protein to plant plasma membrane H(+)-ATPase. The 14-3-3 binding site in the Arabidopsis plasma membrane H(+)-ATPase AHA2 was localized to the three C-terminal residues of the enzyme (Tyr(946)-Thr-Val). Binding of 14-3-3 protein to this target was induced by phosphorylation of Thr(947) (K(D) = 88 nM) and was in practice irreversible in the presence of fusicoccin (K(D) = 7 nM). Mass spectrometry analysis demonstrated that AHA2 expressed in yeast was phosphorylated at Thr(947). We conclude that the extreme end of AHA2 contains an unusual high-affinity binding site for 14-3-3 protein.
authors.affiliation: Department of Plant Biology, Royal Veterinary and Agricultural University, Thorvaldsensvej 40, DK-1871 Frederiksberg, Copenhagen, Denmark.
authors.forename: A T
authors.initials: AT
authors.lastname: Fuglsang
authors.forename: S
authors.initials: S
authors.lastname: Visconti
authors.forename: K
authors.initials: K
authors.lastname: Drumm
authors.forename: T
authors.initials: T
authors.lastname: Jahn
authors.forename: A
authors.initials: A
authors.lastname: Stensballe
authors.forename: B
authors.initials: B
authors.lastname: Mattei
authors.forename: O N
authors.initials: ON
authors.lastname: Jensen
authors.forename: P
authors.initials: P
authors.lastname: Aducci
authors.forename: M G
authors.initials: MG
authors.lastname: Palmgren
mesh_terms: D048948:14-3-3 Proteins; D000595:Amino Acid Sequence; D017360:Arabidopsis / Q000378:metabolism*; D002462:Cell Membrane / Q000378:metabolism; D008969:Molecular Sequence Data; D010766:Phosphorylation; D011506:Proteins / Q000378:metabolism*; D006180:Proton-Translocating ATPases / Q000378:metabolism*; D015398:Signal Transduction; D013912:Threonine; D014443:Tyrosine; D014446:Tyrosine 3-Monooxygenase; D014633:Valine
chemical_list: D048948:14-3-3 Proteins; D011506:Proteins; D013912:Threonine; D014443:Tyrosine; D014446:Tyrosine 3-Monooxygenase; D006180:Proton-Translocating ATPases; D014633:Valine