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FEBS Lett. 2012 Mar 23;586(6):693-8. doi: 10.1016/j.febslet.2012.02.019. Epub 2012 Feb 23.

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

Author information

1
Asian Natural Environmental Science Center (ANESC), The University of Tokyo, Tokyo, Japan.

Abstract

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 α subunit of the SnRK1 protein kinase complex, the β subunits of which are known targets of myristoylation.

PMID:
22449965
DOI:
10.1016/j.febslet.2012.02.019
[Indexed for MEDLINE]
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