ArticleCellular & molecular biology letters2009
The GTPase domain of Galphao contributes to the functional interaction of Galphao with the promyelocytic leukemia zinc finger protein.
Article in Cellular & molecular biology letters, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
1 citing paper in PubMed, 2 citations in OpenAlex.
- The alpha subunit of Go modulates cell proliferation and differentiation through interactions with Necdin.Cell communication and signaling : CCS · 2014Article
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2 authors at 1 institution in 1 country.
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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 (Galphao). Activated Galphao interacts with PLZF and augments its function as a repressor of transcription and cell growth. G protein-coupled receptor-mediated Galphao activation also enhanced PLZF function. In this study, we determined that the GTPase domain of Galphao contributes to Galphao:PLZF interaction. We also showed that the Galphao GTPase domain is important in modulating the function of PLZF. This data indicates that the GTPase domain of Galphao may be necessary for the functional interaction of Galphao with PLZF.
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