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In vivo analysis of Yorkie phosphorylation sites

Open access
Oh, H, Irvine, K D·2009·Oncogene

Abstract

The co-activator Yorkie (Yki) mediates transcriptional regulation effected by the Drosophila Fat–Warts (Wts)–Hippo (Hpo) pathways. Yki is inhibited by Wts-mediated phosphorylation, and a Wts phosphorylation site at Ser168 has been identified. Here we identify two additional Wts phosphorylation sites on Yki, and examine the respective contribution of all three sites to Yki nuclear localization and activity. Our results show that although Ser168 is the most critical site, all three phosphorylation sites influence Yki localization and activity in vivo, and can be sites of regulation by Wts. Thus, investigations of the role of Yki and its mammalian homolog Yes-associated protein (YAP) in development and oncogenesis should include evaluations of additional sites. The WW domains of Yki are not required for its phosphorylation, but instead are positively required for its activity. We also identify two potential sites of phosphorylation by an unknown kinase, which could influence phosphorylation of Ser168 by Wts, suggesting that there are additional mechanisms for regulating Yki/YAP activity.

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Metadata

Authors
Oh, H., & Irvine, K. D.
Venue
Oncogene
Published
2009-03-30
Volume
28
Issue
17
Pages
1916-1927
ISSN
  • 0950-9232 (ISSN-L)
  • 1476-5594
OpenAlex
W2003111150
Cited by
195
References
4
FWCI
6.49
Type
journal article
Language
en
Open access
green

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CoChat. (2026). Citation check: In vivo analysis of Yorkie phosphorylation sites. https://app.cochat.ai/papers/10.1038/onc.2009.43
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Oh, H., & Irvine, K. D. (2009). In vivo analysis of Yorkie phosphorylation sites. Oncogene. https://doi.org/10.1038/onc.2009.43

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