Filling out the Hippo pathway

Saucedo, Leslie; Edgar, Bruce A.

doi:10.1038/nrm2221

Cited by 344 publications

(306 citation statements)

References 91 publications

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“…The SWH pathway controls organ size by modulating cell growth, proliferation, and apoptosis. [24][25][26] Many components of this pathway are conserved from yeast to human and have been implicated in tumor formation. The core components of the SWH pathway are two serine/threonine kinases, Hippo and Warts.…”

Section: Resultsmentioning

confidence: 99%

Phosphoproteome Analysis of Drosophila melanogaster Embryos

et al. 2008

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Protein phosphorylation is a key regulatory event in most cellular processes and development. Mass spectrometry-based proteomics provides a framework for the large-scale identification and characterization of phosphorylation sites. Here, we used a well-established phosphopeptide enrichment and identification strategy including the combination of strong cation exchange chromatography, immobilized metal affinity chromatography, and high-accuracy mass spectrometry instrumentation to study phosphorylation in developing Drosophila embryos. In total, 13 720 different phosphorylation sites were discovered from 2702 proteins with an estimated false-discovery rate (FDR) of 0.63% at the peptide level. Because of the large size of the data set, both novel and known phosphorylation motifs were extracted using the Motif-X algorithm, including those representative of potential ordered phosphorylation events.

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Section: Resultsmentioning

confidence: 99%

Phosphoproteome Analysis of Drosophila melanogaster Embryos

et al. 2008

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“…In flies, members of the Ste20-like kinase, LATS/NDR, and MOB protein families have essential tumour suppressive roles by co-ordination cell growth, proliferation and death [16,[21][22][23]. Considering the impact of initial studies on the Ste20-like Hippo kinase [26,[55][56][57][58], Hippo/Mats/Lats signalling has been referred to as Hippo signalling ever since.…”

Section: Hippo Signalling In G2/m In Drosophila Melanogastermentioning

confidence: 99%

“…Over the past decade Ste20-like kinases, MOB proteins, and LATS/NDR kinases have gained even more attention, since Hippo (a GCK-II Ste20-like kinase), Mats/dMOB1, and Warts/Lats (one of two LATS/NDR kinases in flies) have been established as the central signalling module of the Hippo tumour suppressor signalling cascade in Drosophila melanogaster [21][22][23]. Loss of Hippo, Mats or Warts could be functionally compensated by their mammalian counterparts MST2, LATS1 and MOB1A, respectively [24][25][26], strongly suggesting that, similar to the MEN/SIN, Hippo signalling is very highly conserved from flies to humans.…”

Section: Introductionmentioning

confidence: 99%

Hippo signalling in the G2/M cell cycle phase: Lessons learned from the yeast MEN and SIN pathways

Hergovich

Hemmings

2012

Seminars in Cell & Developmental Biology

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Over the past decade Hippo kinase signalling has been established as an essential tumour suppressor pathway controlling tissue growth in flies and mammals. All members of the Hippo core signalling cassette are conserved from yeast to humans, whereby the yeast analogues of Hippo, Mats and Lats are central components of the mitotic exit network and septation initiation network in budding and fission yeast, respectively. Here, we discuss how far core Hippo signalling components in Drosophila melanogaster and mammals have reported similar mitotic functions as already established for their highly conserved yeast counterparts.

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“…[1][2][3] In mammals, recent studies have established a role for this pathway in regulating cell contact inhibition, organ size control, and cancer development. [4][5][6] The Hippo pathway is activated upon sensing of cell-cell contact via cell surface molecules.…”

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confidence: 99%

c-Abl antagonizes the YAP oncogenic function

et al. 2014

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YES-associated protein (YAP) is a central transcription coactivator that functions as an oncogene in a number of experimental systems. However, under DNA damage, YAP activates pro-apoptotic genes in conjunction with p73. This program switching is mediated by c-Abl (Abelson murine leukemia viral oncogene) via phosphorylation of YAP at the Y357 residue (pY357). YAP as an oncogene coactivates the TEAD (transcriptional enhancer activator domain) family transcription factors. Here we asked whether c-Abl regulates the YAP-TEAD functional module. We found that DNA damage, through c-Abl activation, specifically depressed YAP-TEAD-induced transcription. Remarkably, c-Abl counteracts YAP-induced transformation by interfering with the YAP-TEAD transcriptional program. c-Abl induced TEAD1 phosphorylation, but the YAP-TEAD complex remained unaffected. In contrast, TEAD coactivation was compromised by phosphomimetic YAP Y357E mutation but not Y357F, as demonstrated at the level of reporter genes and endogenous TEAD target genes. Furthermore, YAP Y357E also severely compromised the role of YAP in cell transformation, migration, anchorage-independent growth, and epithelial-to-mesenchymal transition (EMT) in human mammary MCF10A cells. These results suggest that YAP pY357 lost TEAD transcription activation function. Our results demonstrate that YAP pY357 inactivates YAP oncogenic function and establish a role for YAP Y357 phosphorylation in cell-fate decision.

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Filling out the Hippo pathway

Cited by 344 publications

References 91 publications

Phosphoproteome Analysis of Drosophila melanogaster Embryos

Phosphoproteome Analysis of Drosophila melanogaster Embryos

Hippo signalling in the G2/M cell cycle phase: Lessons learned from the yeast MEN and SIN pathways

c-Abl antagonizes the YAP oncogenic function

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