2008
DOI: 10.1002/bies.20757
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Pygopus and the Wnt signaling pathway: A diverse set of connections

Abstract: Identification of Pygopus in Drosophila as a dedicated component of the Wg (fly homolog of mammalian Wnt) signaling cascade initiated many inquiries into the mechanism of its function. Surprisingly, the nearly exclusive role for Pygopus in Wg signal transduction in flies is not seen in mice, where Pygopus appears to have both Wnt-related and Wnt-independent functions. This review addresses the initial findings of Pygopus as a Wg/Wnt co-activator in light of recent data from both fly and mammalian studies. We c… Show more

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Cited by 57 publications
(50 citation statements)
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“…Rather, the consequences of abrogating the interaction are restricted to a late step in spermiogenesis. In an expanding number of contexts in which Pygo2 is being implicated as a modulator of Wnt signaling (Mosimann et al, 2009;Jessen et al, 2008;Chen et al, 2010), our work provides an important piece of the puzzle needed for a holistic understanding. .…”
Section: Research Articlementioning
confidence: 99%
“…Rather, the consequences of abrogating the interaction are restricted to a late step in spermiogenesis. In an expanding number of contexts in which Pygo2 is being implicated as a modulator of Wnt signaling (Mosimann et al, 2009;Jessen et al, 2008;Chen et al, 2010), our work provides an important piece of the puzzle needed for a holistic understanding. .…”
Section: Research Articlementioning
confidence: 99%
“…The Wnt/b-catenin transcription complex component, Pygopus, was originally identified as a protein required for Wnt-dependent transcriptional activation during embryonic development (1). Pygopus is also overexpressed in and is required for the growth of a number of cancer cell lines of diverse origin (2)(3)(4)(5)(6).…”
Section: Introductionmentioning
confidence: 99%
“…The Pygopus (Pygo) family of proteins regulates Wnt/β-catenin signaling by controlling transcription (13) as well as linking this pathway to changes in epigenetic chromatin marks. Pygo proteins directly bind to an active transcriptional histone mark, lysine 4-trimethylated histone H3 (H3K4me3) (14,15).…”
mentioning
confidence: 99%