Regulation of the Hippo–YAP pathway by protease-activated receptors (PARs)

Mo, Jung-Soon; Yu, Fa-Xing; Gong, Rui; Brown, Joan Heller; Guan, Kun‐Liang

doi:10.1101/gad.197582.112

Cited by 251 publications

(286 citation statements)

References 37 publications

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“…3f). Junctional breakage induced by EGTA 19 and the vascular permeability factor, thrombin 20 , also promoted nuclear localization of YAP in confluent ECs (Supplementary Figs 5 and 6 and Fig. 3g,h).…”

Section: Yap Is Expressed In the Ecs Of The Neovascular Regionmentioning

confidence: 79%

Yes-associated protein regulates endothelial cell contact-mediated expression of angiopoietin-2

et al. 2015

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Angiogenesis is regulated by the dynamic interaction between endothelial cells (ECs).Hippo-Yes-associated protein (YAP) signalling has emerged as a key pathway that controls organ size and tissue growth by mediating cell contact inhibition. However, the role of YAP in EC has not been defined yet. Here, we show expression of YAP in the developing front of mouse retinal vessels. YAP subcellular localization, phosphorylation and activity are regulated by VE-cadherin-mediated-EC contacts. This VE-cadherin-dependent YAP phosphorylation requires phosphoinositide 3-kinase-Akt activation. We further identify angiopoietin-2 (ANG-2) as a potential transcriptional target of YAP in regulating angiogenic activity of EC in vitro and in vivo. Overexpression of YAP-active form in EC enhances angiogenic sprouting, and this effect is blocked by ANG-2 depletion or soluble Tie-2 treatment. These findings implicate YAP as a critical regulator in angiogenesis and provide new insights into the mechanism coordinating junctional stability and angiogenic activation of ECs.

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Section: Yap Is Expressed In the Ecs Of The Neovascular Regionmentioning

confidence: 79%

Yes-associated protein regulates endothelial cell contact-mediated expression of angiopoietin-2

et al. 2015

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“…Furthermore, WWC1 (Kibra orthologs) (20 -22), NF2 (Merlin orthologs) (23)(24)(25) and FRMD6 (Expanded orthologs) (26) have been identified as upstream regulators for the core kinase cascade. Although the upstream receptors are still elusive, recent studies suggest that GPCR (27) and protease-activated receptors (28,29) may be the upstream components that link extracellular signals to activation of the Hippo pathway in mammals.…”

mentioning

confidence: 99%

Defining the Protein–Protein Interaction Network of the Human Hippo Pathway

Wang

Huang

et al. 2014

Molecular & Cellular Proteomics

123

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The Hippo pathway, which is conserved from Drosophila to mammals, has been recognized as a tumor suppressor signaling pathway governing cell proliferation and apoptosis, two key events involved in organ size control and tumorigenesis. Although several upstream regulators, the conserved kinase cascade and key downstream effectors including nuclear transcriptional factors have been defined, the global organization of this signaling pathway is not been fully understood. Thus, we conducted a proteomic analysis of human Hippo pathway, which revealed the involvement of an extensive protein-protein interaction network in this pathway. The mass spectrometry data were deposited to ProteomeXchange with identifier PXD000415. Our data suggest that 550 interactions within 343 unique protein components constitute the central protein-protein interaction landscape of human Hippo pathway. Our study provides a glimpse into the global organization of Hippo pathway, reveals previously unknown interactions within this pathway, and uncovers new potential components involved in the regulation of this pathway. Understanding these interactions will help us further dissect the Hippo signaling-pathway and extend our knowledge of organ size control. Molecular &

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“…At the center stage of this pathway is the Mst1/2-Lats1/2 kinase cascade. Upstream signals such as cell adhesion, cytoskeleton remodeling, lysophosphatidic acid (LPA) 2 and its respective G-protein-coupled receptors (GPCRs) were found to regulate the Hippo pathway (15)(16)(17)(18)(19)(20)(21)(22)(23). YAP transcription co-activator and its paralog TAZ are the best known Hippo pathway targets mediating gene expression regulation and organ size control (22, 24 -27).…”

mentioning

confidence: 99%

Phosphorylation of Angiomotin by Lats1/2 Kinases Inhibits F-actin Binding, Cell Migration, and Angiogenesis

Dai

She

Chi

et al. 2013

Journal of Biological Chemistry

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140

133

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Background: Substrates of the Hippo pathway kinases Lats1/2 are largely unknown besides YAP/TAZ. Results: Phosphorylation of angiomotin by Lats1/2 inhibits interaction with F-actin thus impairs cell migration and angiogenesis. Conclusion: AMOTp130 is a physiological and functional substrate of Lats1/2 and the Hippo pathway. Significance: Demonstrating how identification of novel substrates would facilitate understanding the physiology of the Hippo pathway.

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Regulation of the Hippo–YAP pathway by protease-activated receptors (PARs)

Cited by 251 publications

References 37 publications

Yes-associated protein regulates endothelial cell contact-mediated expression of angiopoietin-2

Yes-associated protein regulates endothelial cell contact-mediated expression of angiopoietin-2

Defining the Protein–Protein Interaction Network of the Human Hippo Pathway

Phosphorylation of Angiomotin by Lats1/2 Kinases Inhibits F-actin Binding, Cell Migration, and Angiogenesis

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