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Mary J. Cismowski

Researcher at Nationwide Children's Hospital

Publications -  38
Citations -  1485

Mary J. Cismowski is an academic researcher from Nationwide Children's Hospital. The author has contributed to research in topics: Heterotrimeric G protein & Signal transduction. The author has an hindex of 19, co-authored 38 publications receiving 1347 citations. Previous affiliations of Mary J. Cismowski include The Research Institute at Nationwide Children's Hospital & Neurocrine Biosciences.

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Receptor-independent activators of heterotrimeric g-protein signaling pathways

TL;DR: AGS proteins provide unexpected mechanisms for input to heterotrimeric G-protein signaling pathways and may also serve as novel binding partners for Gα and Gβγ that allow the subunits to subserve functions that do not require initialheterotrimer formation.
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Genetic screens in yeast to identify mammalian nonreceptor modulators of G-protein signaling.

TL;DR: A cDNA product identified from the inhibitor screen encodes a previously identified regulator of G-protein signaling, human RGS5, and appears to function by facilitating guanosine triphosphate (GTP) exchange on the heterotrimeric Gα.
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Activation of heterotrimeric G-protein signaling by a ras-related protein. Implications for signal integration.

TL;DR: The in vivo and in vitro properties of AGS1 are consistent with it functioning as a direct guanine nucleotide exchange factor for Gαi/Gαo heterotrimeric signaling pathways, which presents a unique mechanism for signal integration via heterOTrimeric G-protein signaling pathways.
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Receptor-independent activators of heterotrimeric G-proteins.

TL;DR: Using a functional screen based upon the pheromone response pathway in Saccharomyces cerevisiae, three proteins were identified, AGS1-3 (for Activators of G-protein Signalling), that activated heterotrimeric G- protein signalling pathways in the absence of a typical receptor.