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Tyrosine Phosphorylation Inhibits the Interaction of 14‐3‐3 Proteins with the Plant Plasma Membrane H + ‐ATPase
Author(s) -
Giacometti S.,
Camoni L.,
Albumi C.,
Visconti S.,
De Michelis M. I.,
Aducci P.
Publication year - 2004
Publication title -
plant biology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.871
H-Index - 87
eISSN - 1438-8677
pISSN - 1435-8603
DOI - 10.1055/s-2004-820933
Subject(s) - protein tyrosine phosphatase , phenylarsine oxide , biology , phosphorylation , tyrosine , tyrosine phosphorylation , biochemistry , receptor tyrosine kinase , insulin receptor , tyrosine kinase , atpase , sh2 domain , gene isoform , microbiology and biotechnology , enzyme , receptor , insulin , endocrinology , insulin resistance , gene
Interaction of 14‐3‐3 proteins with their targets depends not only on the phosphorylation status of the target but also on that of 14‐3‐3 Fu et al., 2000). In this work we demonstrated that the maize 14‐3‐3 isoform GF14‐6 is a substrate of the tyrosine kinase insulin growth factor receptor 1. By means of site‐directed mutants of GF14‐6, we identified Tyr‐137 as the specific tyrosine residue phosphorylated by the insulin growth factor receptor 1. Phosphorylation of GF14‐6 on Tyr‐137 lowered its affinity for a peptide mimicking the 14‐3‐3 binding site of the plant plasma membrane H + ‐ATPase. Moreover, phosphorylation in planta of 14‐3‐3 tyrosine residues, resulting from incubation with the tyrosine phosphatase inhibitor, phenylarsine oxide, decreased their association to the H + ‐ATPase.