Characterization and tissue-specific expression of human GSK-3-binding proteins FRAT1 and FRAT2 (Q28208447)

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object named as

Sarah J Freemantle

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Michael J Spinella

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object named as

Michael J Spinella

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author name string

Holly B Portland

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Katherine Ewings

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Florence Dmitrovsky

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Keith DiPetrillo

Phosphorylation-dependent regulation of cyclin D1 nuclear export and cyclin D1-dependent cellular transformation

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language of work or name

English

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publication date

29 May 2002

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published in

Gene

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volume

291

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issue

1-2

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page(s)

17-27

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cites work

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Glycogen synthase kinase-3beta regulates cyclin D1 proteolysis and subcellular localization

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Missing links in GSK3 regulation.

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GSK-3: new thoughts on an old enzyme

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Glycogen synthase kinase-3 enhances nuclear export of a Dictyostelium STAT protein.

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Requirement for glycogen synthase kinase-3beta in cell survival and NF-kappaB activation

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Activation of a novel proto-oncogene, Frat1, contributes to progression of mouse T-cell lymphomas

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In vivo analysis of Frat1 deficiency suggests compensatory activity of Frat3

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GSK3, a master switch regulating cell-fate specification and tumorigenesis

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Posttranslational regulation of cyclin D1 by retinoic acid: a chemoprevention mechanism

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Axin and Frat1 interact with dvl and GSK, bridging Dvl to GSK in Wnt-mediated regulation of LEF-1.

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The role of GSK3beta in regulating neuronal differentiation in Xenopus laevis

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Molecular cloning and characterization of FRAT2, encoding a positive regulator of the WNT signaling pathway

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Retinoic acid promotes ubiquitination and proteolysis of cyclin D1 during induced tumor cell differentiation

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Conservation of intracellular Wnt signaling components in dorsal-ventral axis formation in zebrafish

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Presenilin 1 associates with glycogen synthase kinase-3beta and its substrate tau

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A GSK3-binding peptide from FRAT1 selectively inhibits the GSK3-catalysed phosphorylation of axin and beta-catenin

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RNA processing and the control of spermatogenesis

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Protein kinase FA/GSK-3 phosphorylates tau on Ser235-Pro and Ser404-Pro that are abnormally phosphorylated in Alzheimer's disease brain.

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GBP, an inhibitor of GSK-3, is implicated in Xenopus development and oncogenesis

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