Two Pdk1 phosphorylation sites on the plant cell death suppressor Adi3 contribute to substrate phosphorylation |
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Authors: | Joel W. Gray Anna C. Nelson Dittrich Sixue Chen Julian Avila Patrick Giavalisco Timothy P. Devarenne |
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Affiliation: | 1. Department of Biochemistry and Biophysics, Texas A&M University, College Station, TX, 77843, USA;2. Department of Biology, Genetics Institute, Plant Molecular and Cellular Biology Program, Interdisciplinary Center for Biotechnology Research, University of Florida, Gainesville, FL 32610, USA;3. Max Planck Institute of Molecular Plant Physiology, 14476 Glom-Potsdam, Germany |
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Abstract: | The tomato AGC kinase Adi3 is phosphorylated by Pdk1 for activation of its cell death suppression activity. The Pdk1 phosphorylation site for activation of Adi3 is at Ser539. However, there is at least one additional Pdk1 phosphorylation site on Adi3 that has an unknown function. Here we identify an Arabidopsis thaliana sequence homologue of Adi3 termed AGC1-3. Two Pdk1 phosphorylation sites were identified on AGC1-3, activation site Ser596 and Ser269, and by homology Ser212 on Adi3 was identified as a second Pdk1 phosphorylation site. While Ser212 is not required for Adi3 autophosphorylation, Ser212 was shown to be required for full phosphorylation of the Adi3 substrate Gal83. |
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Keywords: | Adi3, AvrPto-dependent Pto-interacting protein 3 Gal83, galactose-specific gene 83 MBP, maltose binding protein Pdk1, 3-phosphoinositide dependent protein kinase 1 PCD, programmed cell death SnRK1, Sucrose non-Fermenting-1-Related Protein Kinase 1 |
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