期刊
PLANT CELL
卷 27, 期 3, 页码 711-723出版社
AMER SOC PLANT BIOLOGISTS
DOI: 10.1105/tpc.114.135335
关键词
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资金
- National Basic Research and Development Program of China [2011CB100303]
- Ministry of Science and Technology of China [2012AA10A302]
- Ministry of Agriculture of China [2011ZX08001-005, 2013ZX08001-005, 2014ZX08001005]
- Ministry of Education and Bureau of Foreign Experts of China [B14027]
- National Natural Science Foundation of China [31322048]
- Ministry of Education, Culture, Sports, Science, and Technology of Japan [22119002]
Phosphate transporters (PTs) mediate phosphorus uptake and are regulated at the transcriptional and posttranslational levels. In one key mechanism of posttranslational regulation, phosphorylation of PTs affects their trafficking from the endoplasmic reticulum (ER) to the plasma membrane. However, the kinase(s) mediating PT phosphorylation and the mechanism leading to ER retention of phosphorylated PTs remain unclear. In this study, we identified a rice (Oryza sativa) kinase subunit, CK2 beta 3, which interacts with PT2 and PT8 in a yeast two-hybrid screen. Also, the CK2 alpha 3/beta 3 holoenzyme phosphorylates PT8 under phosphate-sufficient conditions. This phosphorylation inhibited the interaction of PT8 with PHOSPHATE TRANSPORTER TRAFFIC FACILITATOR1, a key cofactor regulating the exit of PTs from the ER to the plasma membrane. Additionally, phosphorus starvation promoted CK2 beta 3 degradation, relieving the negative regulation of PT phosphorus-insufficient conditions. In accordance, transgenic expression of a nonphosphorylatable version of OsPT8 resulted in elevated levels of that protein at the plasma membrane and enhanced phosphorus accumulation and plant growth under various phosphorus regimes. Taken together, these results indicate that CK2 alpha 3/beta 3 negatively regulates PTs and phosphorus status regulates CK2 alpha 3/beta 3.
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