| References |
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| REF 1 |
LATS2-Ajuba complex regulates gamma-tubulin recruitment to centrosomes and spindle organization during mitosis. FEBS Lett. 2006 Feb 6;580(3):782-8.
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| REF 2 |
Ajuba LIM proteins are negative regulators of the Hippo signaling pathway. Curr Biol. 2010 Apr 13;20(7):657-62.
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| REF 3 |
Protein interaction network of the mammalian Hippo pathway reveals mechanisms of kinase-phosphatase interactions. Sci Signal. 2013 Nov 19;6(302):rs15.
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| REF 4 |
The tumor suppressor Lats2 is pivotal in Aurora A and Aurora B signaling during mitosis. Cell Cycle. 2011 Aug 15;10(16):2724-36.
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| REF 5 |
The centrosomal protein Lats2 is a phosphorylation target of Aurora-A kinase. Genes Cells. 2004 May;9(5):383-97.
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| REF 6 |
OncoPPi-informed discovery of mitogen-activated protein kinase kinase 3 as a novel binding partner of c-Myc. Oncogene. 2017 Oct 19;36(42):5852-5860.
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| REF 7 |
Enabling systematic interrogation of protein-protein interactions in live cells with a versatile ultra-high-throughput biosensor platform. J Mol Cell Biol. 2016 Jun;8(3):271-81.
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| REF 8 |
Roles of mammalian sterile 20-like kinase 2-dependent phosphorylations of Mps one binder 1B in the activation of nuclear Dbf2-related kinases. Genes Cells. 2009 Dec;14(12):1369-81.
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| REF 9 |
Deubiquitylase USP9X suppresses tumorigenesis by stabilizing large tumor suppressor kinase 2 (LATS2) in the Hippo pathway. J Biol Chem. 2018 Jan 26;293(4):1178-1191.
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| REF 10 |
Deubiquitinating Enzyme USP9X Suppresses Tumor Growth via LATS Kinase and Core Components of the Hippo Pathway. Cancer Res. 2017 Sep 15;77(18):4921-4933.
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| REF 11 |
Negative regulation of YAP by LATS1 underscores evolutionary conservation of the Drosophila Hippo pathway. Cancer Res. 2008 Apr 15;68(8):2789-94.
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| REF 12 |
Cytoplasmic ASPP1 inhibits apoptosis through the control of YAP. Genes Dev. 2010 Nov 1;24(21):2430-9.
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| REF 13 |
The Lats2 tumor suppressor augments p53-mediated apoptosis by promoting the nuclear proapoptotic function of ASPP1. Genes Dev. 2010 Nov 1;24(21):2420-9.
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| REF 14 |
Mst2 and Lats kinases regulate apoptotic function of Yes kinase-associated protein (YAP). J Biol Chem. 2008 Oct 10;283(41):27534-46.
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| REF 15 |
Hippo pathway-dependent and -independent roles of RASSF6. Sci Signal. 2009 Sep 29;2(90):ra59.
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| REF 16 |
Angiomotin family proteins are novel activators of the LATS2 kinase tumor suppressor. Mol Biol Cell. 2011 Oct;22(19):3725-33.
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| REF 17 |
Role of Angiomotin-like 2 mono-ubiquitination on YAP inhibition. EMBO Rep. 2016 Jan;17(1):64-78.
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| REF 18 |
Ski regulates Hippo and TAZ signaling to suppress breast cancer progression. Sci Signal. 2015 Feb 10;8(363):ra14.
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| REF 19 |
Regulation of the Hippo-YAP pathway by G-protein-coupled receptor signaling. Cell. 2012 Aug 17;150(4):780-91.
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| REF 20 |
Src Inhibits the Hippo Tumor Suppressor Pathway through Tyrosine Phosphorylation of Lats1. Cancer Res. 2017 Sep 15;77(18):4868-4880.
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| REF 21 |
Serum deprivation inhibits the transcriptional co-activator YAP and cell growth via phosphorylation of the 130-kDa isoform of Angiomotin by the LATS1/2 protein kinases. Proc Natl Acad Sci U S A. 2013 Oct 22;110(43):17368-73.
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| REF 22 |
Actin-binding and cell proliferation activities of angiomotin family members are regulated by Hippo pathway-mediated phosphorylation. J Biol Chem. 2013 Dec 27;288(52):37296-307.
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| REF 23 |
Phosphorylation of angiomotin by Lats1/2 kinases inhibits F-actin binding, cell migration, and angiogenesis. J Biol Chem. 2013 Nov 22;288(47):34041-51.
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| REF 24 |
Differential NDR/LATS interactions with the human MOB family reveal a negative role for human MOB2 in the regulation of human NDR kinases. Mol Cell Biol. 2010 Sep;30(18):4507-20.
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| REF 25 |
The characterisation of LATS2 kinase regulation in Hippo-YAP signalling. Cell Signal. 2016 May;28(5):488-497.
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| REF 26 |
LATS2 suppresses oncogenic Wnt signaling by disrupting -catenin/BCL9 interaction. Cell Rep. 2013 Dec 26;5(6):1650-63.
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| REF 27 |
JCAD Promotes Progression of Nonalcoholic Steatohepatitis to Liver Cancer by Inhibiting LATS2 Kinase Activity. Cancer Res. 2017 Oct 1;77(19):5287-5300.
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