The Ste20-like kinase Mst2 activates the human large tumor suppressor kinase Lats1
By Eunice H. Y. Chan, M. Nousiainen, Ravindra B. Chalamalasetty, A. Schäfer, Erich A. Nigg, H. Silljé. Oncogene, 2005
626 citations recorded by the source corpus.
Subfields: Cell Biology, Molecular Biology
View Paper: https://www.semanticscholar.org/paper/a51d0640986da48291689252d17c7e65bad3f711
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Citations in the corpus
- The Hippo pathway in organ size control, tissue regeneration and stem cell self-renewal (2011, positive): “Activation of Mst1/2 leads to phosphorylation and activation of their direct substrates, Lats1/2 (ref”
- The Hippo signaling pathway coordinately regulates cell proliferation and apoptosis by inactivating Yorkie, the Drosophila Homolog of YAP. (2005, background): “Indeed, a recent study has demonstrated the activation of the mammalian Lats1 kinase by the mammalian Hpo homologs Mst1/Mst2 (Chan et al., 2005).”
- Mst1 and Mst2 maintain hepatocyte quiescence and suppress the development of hepatocellular carcinoma through inactivation of the Yap1 oncogene (2009, background): “…and the ability of Mst1/2 to phosphorylate Lats1/2 and Mob1, as well as Lats1 phosphorylation and inhibition of Yap1, the mammalian ortholog of Yorkie, have been observed in vitro and in cell culture (Chan et al., 2005; Dong et al., 2007; Hao et al., 2008; Praskova et al., 2008; Zhao et al., 2007).”
- The nuts and bolts of AGC protein kinases (2010, neutral): “MST1 (also known as STK4) and MST2 (also known as STK3) phosphorylate LATS1 and LATS2 (Ref”
- The Hippo pathway: regulators and regulations. (2013, background): “Core Hippo pathway: a kinase cascade MST1/2 are STE20 family protein kinases and can phosphorylate Sav1, Lats1/2, and Mob1 (Wu et al. 2003; Chan et al. 2005; Callus et al. 2006; Praskova et al. 2008).”
- Cell detachment activates the Hippo pathway via cytoskeleton reorganization to induce anoikis. (2012, background): “Lats1/2 are activated by phosphorylation of the activation loop (S909/872 for Lats1 and Lats2) and the hydrophobic motif (T1079/999 for Lats1 and Lats2) (Chan et al. 2005).”
- Identification and validation of oncogenes in liver cancer using an integrative oncogenomic approach. (2006, background): “Interestingly, mammalian homologs exist for most Hippo pathway members (Chan et al., 2005; Tamaskovic et al., 2003), some of which have previously been linked to cancer development (e.”
- Mechanisms of Hippo pathway regulation (2016, positive): “However, the exact role of NDR1/2 in Hippo pathway regulation still needs to be further defined, as deletion of LATS1/2 is sufficient to abolish YAP phosphorylation and cause constitutive YAP nuclear localization under most conditions examined (Meng et al. 2015).”
- Hippo Pathway in Organ Size Control, Tissue Homeostasis, and Cancer. (2015, positive): “Furthermore, phosphorylation of MOB1 by MST1/2 enhances MOB1 interaction with the autoinhibitory domain of LATS1/2, leading to full activation of LATS1/ 2 (Callus et al., 2006; Chan et al., 2005; Praskova et al., 2004; Wu et al., 2003).”
- The Hippo signalling pathway and its implications in human health and diseases (2022, background): “SuperHippo, a designed WWC-derived protein, was shown to inhibit YAP/TAZ activity by inducing the phosphorylation of LATS1/2 due to the requirement of the WWC protein in the activation of LATS1/2.”
- Angiomotin is a novel Hippo pathway component that inhibits YAP oncoprotein. (2011, background): “Core to the Hippo pathway is a kinase cascade in which mammalian Mst1/2 kinases (Drosophila Hippo homologs) complexed with a scaffold protein, Sav1, to phosphorylate and activate the Lats1/2 kinases (Chan et al. 2005; Callus et al. 2006).”
- The Hippo Signaling Pathway in Development and Cancer (2010, background): “These proteins form a conserved kinase cassette (Callus et al., 2006; Praskova et al., 2008; Chan et al., 2005) that phosphorylates and inactivates the mammalian Yki homologs YAP (Dong et al.”
- The Hippo-YAP pathway in organ size control and tumorigenesis: an updated version. (2010, background): “Current data suggest that the hydrophobic motif of Lats1/2 is phosphorylated by Mst1/2, and the activation loop is autophosphorylated (Fig. 2; Chan et al. 2005).”