G protein beta2 subunit interacts directly with neuropathy target esterase and r

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Int J Biochem Cell Biol. 2006 Aug 14

G protein beta2 subunit interacts directly with neuropathy target

esterase and regulates its activity.

Chen R, Chang PA, Long DX, Liu CY, Yang L, Wu YJ.

Laboratory of Molecular Toxicology, State Key Laboratory of

Integrated Management of Pest Insects and Rodents, Institute of

Zoology, Chinese Academy of Sciences, Beijing 100080, PR China;

Graduate School of the Chinese Academy of Sciences, Beijing 100039,

PR China.

Neuropathy target esterase (NTE) was identified as the primary target

of organophosphate compounds that cause a delayed neuropathy with

degeneration of nerve axons. NTE is a novel phospholipase B anchored

to the cytoplasmic face of endoplasmic reticulum and essential for

embryonic and nervous development. However, little is known about the

regulation of NTE. A human fetal brain cDNA library was screened for

proteins that interact with NTE, Gbeta2 and Gbeta2-like I subunits

were found to be able to bind the C-terminal of NTE in yeast. The

interaction of Gbeta2 and NTE was confirmed by in vivo co-

immunoprecipitation analysis in COS7 cells. Furthermore, depletion of

Gbeta2 by RNA interference down regulated the activity of NTE but not

its expression level. In addition, the activity of NTE was down

regulated by the G protein signal pathway influencing factor,

pertussis toxin, treatment in vivo. These findings suggest that

Gbeta2 may play a significant role in maintaining the activity of NTE.