TAZ: a novel transcriptional co‐activator regulated by interactions with 14‐3‐3 and PDZ domain proteins

By F. Kanai, P. Marignani, Dilara Sarbassova, Ryohei Yagi, R. Hall, M. Donowitz, Akihiko Hisaminato, Tsutomu Fujiwara, Yoshiaki Ito, Lewis C. Cantley and 1 more. EMBO Journal, 2000

758 citations recorded by the source corpus.

Subfields: Molecular Biology

View Paper: https://www.semanticscholar.org/paper/351bb8a44f2b5a46670f652d0326e39a703f7c9c

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In Molecular Biology

1. K. Guan
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Citations in the corpus

• Hippo pathway effector Yap promotes cardiac regeneration (2013, background): “Yap shares 45% amino acid identity with Taz (35), but the potential functional redundancy of these proteins has not been examined through compound loss of function mutations in mice.”
• Global Analysis of DELLA Direct Targets in Early Gibberellin Signaling in Arabidopsis[W] (2007, background): “BT4 has two protein–protein interaction domains: a BTB/POZ domain for dimer or oligomer formation and a zinc finger TAZ domain that is present in transcriptional modulators (Kanai et al., 2000; Du and Poovaiah, 2004).”
• The biology of YAP/TAZ: hippo signaling and beyond. (2014, background): “indicated a requirement for the COOH-terminal portion of YAP and TAZ for transcription (99, 209).”
• YAP/TAZ at the roots of cancer (2016, background): “Yaffe (Kanai et al., 2000; Sudol, 1994), but their function started to be understood only after it became clear that they were homologue of Drosophila Yorkie, the nuclear mediator of the Drosophila Hippo cascade (Huang et al.”
• Effects of dexamethasone, ascorbic acid and β-glycerophosphate on the osteogenic differentiation of stem cells in vitro (2013, background): “TAZ contains a coiled-coil carboxy-terminal domain that recruits core components of the transcriptional machinery and a specific domain that binds to the Pro-Pro-X-Tyr motif (where X is any amino acid) of Runx2 [17,18].”
• TAZ Promotes Cell Proliferation and Epithelial-Mesenchymal Transition and Is Inhibited by the Hippo Pathway (2008, background): “Additionally, it has also been reported that TAZ is a phosphoprotein, and phosphorylation likely regulates TAZ interaction with 14-3-3 and subcellular localization (13).”
• The Hippo pathway effectors TAZ and YAP in development, homeostasis and disease (2014, background): “The finding that TAZ phosphorylation on a conserved serine residue (Ser89 in human TAZ; equivalent to Ser127 in human YAP) promotes binding to 14-3-3 proteins and subsequent cytoplasmic retention revealed a key mechanism of Hippo pathway function (Kanai et al., 2000).”
• The Hippo-YAP pathway in organ size control and tumorigenesis: an updated version. (2010, background): “YAP and TAZ mRNA is expressed in a wide range of tissues, except peripheral blood leukocytes (Kanai et al. 2000; Komuro et al. 2003).”
• TEAD/TEF transcription factors utilize the activation domain of YAP65, a Src/Yes-associated protein localized in the cytoplasm. (2001, background): “3-3 binding domain (Kanai et al. 2000),”
• The Hippo pathway: regulators and regulations. (2013, background): “Also, TAZ and Yki are phosphorylated by Lats1/2 or Wts, respectively, on multiple HXRXXS sites (Kanai et al. 2000; Dong et al. 2007; Lei et al. 2008; Oh and Irvine 2008; Ren et al. 2010b).”