A putative myristoylated 2C-type protein phosphatase, PP2C74, interacts with SnRK1 in Arabidopsis

详细信息    查看全文

• 作者：Daisuke Tsugama^a ; Shenkui Liu^b ; Tetsuo Takano^a ; ^{takano@anesc.u-tokyo.ac.jp}
• 关键词：SnRK ; sucrose non-fermenting-1-related protein kinase ; PP2C ; 2C-type protein phosphatase ; AKIN10 ; Arabidopsis SNF1 kinase homolog 10 ; MYR ; N-myristoylation ; NMT ; N-myristoyltransferase ; MAMP ; microbe-associated molecular pattern ; qRT-PCR ; quantitative rev
• 刊名：FEBS Letters
• 出版年：2012
• 出版时间：23 March, 2012
• 年：2012
• 卷：586
• 期：6
• 页码：693-698
• 全文大小：617 K

文摘

N-myristoylation is a lipid modification of many signaling proteins in which myristate is added to an N-terminal glycine residue. Here we show that PP2C74, a putative myristoylated 2C-type protein phosphatase (PP2C) in Arabidopsis, is transcribed in various tissues and has protein phosphatase activity. GFP-fused PP2C74 localized to the plasma membrane, but not when a glycine residue at position 2, which is the putative myristoylation site, was substituted with an alanine residue. Yeast two-hybrid analysis and GST pull-down analysis showed that PP2C74 interacts with AKIN10, the catalytic ¦Á subunit of the SnRK1 protein kinase complex, the ¦Â subunits of which are known targets of myristoylation.

Structured summary of protein interactions

with by ()

with by ()