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. 2008 Oct 16;14(1):46. doi: 10.2478/s11658-008-0033-6

The GTPase domain of Galphao contributes to the functional interaction of Galphao with the promyelocytic leukemia zinc finger protein

Jung Hee Won 2, Sung Ho Ghil 2,✉
PMCID: PMC6275613  PMID: 18953495

Abstract

Go, one of the most abundant heterotrimeric G proteins in the brain, is classified as a member of the Gi/Go family based on its homology to Gi proteins. Recently, we identified promyelocytic leukemia zinc finger protein (PLZF) as a candidate downstream effector for the alpha subunit of Go (Gαo). Activated Gαo interacts with PLZF and augments its function as a repressor of transcription and cell growth. G protein-coupled receptor-mediated Gαo activation also enhanced PLZF function. In this study, we determined that the GTPase domain of Gαo contributes to Gαo:PLZF interaction. We also showed that the Gαo GTPase domain is important in modulating the function of PLZF. This data indicates that the GTPase domain of Gαo may be necessary for the functional interaction of Gαo with PLZF.

Key words: Cell growth, Differentiation, Domain, G protein

Full Text

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Abbreviations used

β-gal

β-galactosidase

BrdU

bromodeoxyuridine

Gαo

the alpha subunit of Go

G proteins

heterotrimeric GTP-binding proteins

GST

glutathione-S-transferase

PKA

cAMP-dependent protein kinase

PLZF

promyelocytic leukemia zinc finger protein

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