Two Pdk1 phosphorylation sites on the plant cell death suppressor Adi3 contribute to substrate phosphorylation. Academic Article

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.

authors

• Devarenne, Timothy

published proceedings

• Biochim Biophys Acta

author list (cited authors)

• Gray, J. W., Nelson Dittrich, A. C., Chen, S., Avila, J., Giavalisco, P., & Devarenne, T. P.

citation count

• 4

complete list of authors

• Gray, Joel W||Nelson Dittrich, Anna C||Chen, Sixue||Avila, Julian||Giavalisco, Patrick||Devarenne, Timothy P

publication date

• January 2013

publisher

• Elsevier  Publisher

published in

• Biochimica et Biophysica Acta: international journal of biochemistry and biophysics  Journal

keywords

• 3-phosphoinositide-dependent Protein Kinases
• Amino Acid Sequence
• Arabidopsis
• Catalytic Domain
• Cell Death
• Molecular Sequence Data
• Mutation
• Phosphorylation
• Plant Cells
• Plant Proteins
• Protein Serine-threonine Kinases
• Sequence Homology, Amino Acid
• Solanum Lycopersicum

Digital Object Identifier (DOI)

• 10.1016/j.bbapap.2013.03.006

start page

• 1099

end page

• 1106

volume

• 1834

issue

• 6

URL

• http%3A%2F%2Fdx.doi.org%2F10.1016%2Fj.bbapap.2013.03.006