Journal
JOURNAL OF BIOLOGICAL CHEMISTRY
Volume 288, Issue 47, Pages 34041-34051Publisher
AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
DOI: 10.1074/jbc.M113.518019
Keywords
Actin; Angiogenesis; Cell Migration; Protein Kinases; Protein Phosphorylation; Lats; AMOT; Protein Kinase; the Hippo Pathway
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Funding
- National Natural Science Foundation of China [31271508]
- State Key Development Program for Basic Research of China [2013CB945303]
- Natural Science Foundation of Zhejiang [LR12C07001]
- Thousand Young Talents Plan of China
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The Hippo tumor suppressor pathway plays important roles in organ size control through Lats1/2 mediated phosphorylation of the YAP/TAZ transcription co-activators. However, YAP/TAZ independent functions of the Hippo pathway are largely unknown. Here we report a novel role of the Hippo pathway in angiogenesis. Angiomotin p130 isoform (AMOTp130) is phosphorylated on a conserved HXRXXS motif by Lats1/2 downstream of GPCR signaling. Phosphorylation disrupts AMOT interaction with F-actin and correlates with reduced F-actin stress fibers and focal adhesions. Furthermore, phosphorylation of AMOT by Lats1/2 inhibits endothelial cell migration in vitro and angiogenesis in zebrafish embryos in vivo. Thus AMOT is a direct substrate of Lats1/2 mediating functions of the Hippo pathway in endothelial cell migration and angiogenesis.
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