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Gregory B. Fralish

Researcher at Duke University

Publications -  5
Citations -  368

Gregory B. Fralish is an academic researcher from Duke University. The author has contributed to research in topics: Smoothened & Signal transduction. The author has an hindex of 5, co-authored 5 publications receiving 353 citations. Previous affiliations of Gregory B. Fralish include Howard Hughes Medical Institute.

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Smoothened signal transduction is promoted by G protein-coupled receptor kinase 2.

TL;DR: It is found that G protein-coupled receptor kinase 2 (GRK2) promotes the association between active Smoothened and β-arrestin 2, and Gli-dependent signaling, mediated by coexpression of Smoothensed and GRK2, is diminished by β-arsenin 2 knockdown with shRNA.
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Beta-arrestin 2 regulates zebrafish development through the hedgehog signaling pathway.

TL;DR: It is shown that the functional knockdown of β-arrestin 2 in zebrafish embryos recapitulates the many phenotypes of Hh pathway mutants and suggests that a functional interaction betweenβ-ar Arrestin 2 and Smoothened may be critical to regulate Hh signaling in zbrafish development.
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Smoothened Signaling in Vertebrates Is Facilitated by a G Protein-coupled Receptor Kinase

TL;DR: Results obtained in zebrafish and mice suggest that a GRK functions as a vertebrate kinase for Smoothened, promoting Hedgehog signal transduction during early development.
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Grk5l controls heart development by limiting mTOR signaling during symmetry breaking.

TL;DR: It is found that the zebrafish homolog of mammalian G protein-coupled receptor kinase 5 (GRK5) employs noncanonical, receptor-independent functions to secure symmetry breaking, which could implicate GRK5 as a susceptibility allele for certain cases of CHD.
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N-terminal Tyrosine Modulation of the Endocytic Adaptor Function of the β-Arrestins

TL;DR: It is shown that corresponding N-terminal (Y/F)VTL sequences in β-arrestin1 and -2 differentially regulate μ-adaptin binding and that these naturally occurring variations in β -arrestins may also differentially regulates the composition of the signaling complexes organized on the receptor.