期刊
FEBS LETTERS
卷 589, 期 21, 页码 3321-3327出版社
ELSEVIER SCIENCE BV
DOI: 10.1016/j.febslet.2015.09.025
关键词
Serine/threonine protein kinase; Tyrosine protein kinase; Dual specificity protein kinase; Phosphorylation; Phosphopeptide
资金
- King Abdullah University of Science and Technology (KAUST) - Saudi Arabia
- University of Cambridge - United Kingdom
Yak1 is a member of dual-specificity Tyr phosphorylation-regulated ki nases (DYRKs) that are evolutionarily conserved. The downstream targets of Yak1 and their functions are largely unknown. Here, a homologous protein AtYAK1 was identified in Arabidopsis thaliana and the phosphoprotein profiles of the wild type and an atyak1 mutant were compared on two-dimensional gel following Pro-Q Diamond phosphoprotein gel staining. Annexin1, Annexin2 and RBD were phosphorylated at serine/threonine residues by the AtYak1 kinase. Annexin1, Annodn2 and Annexin4 were also phosphorylated at tyrosine residues. Our study demonstrated that AtYak1 is a dual specificity protein kinase in Arabidopsis that may regulate the phosphorylation status of the annexin family proteins. (C) 2015 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
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