Yes-associated protein (YAP65) interacts with Smad7 and potentiates its inhibitory activity against TGF-β/Smad signaling

Ferrigno, Olivier; Lallemand, François; Verrecchia, Franck; L’Hoste, Sébastien; Camonis, Jacques; Atfi, Azeddine; Mauviel, Alain

doi:10.1038/sj.onc.1205623

Cited by 201 publications

(160 citation statements)

References 23 publications

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“…This suggests that the YAP WW domain, along with an as yet uncharacterized region, has a role in the SMAD7 interaction. YAP was shown to promote the recruitment of SMAD7 to a constitutively active TGFb receptor I, thereby augmenting the repressive role that SMAD7 has in mediating SMAD3/4-driven transcription (Ferrigno et al, 2002). Hence, these data identified YAP as a SMAD7-binding partner with the potential to repress TGFb/SMAD signaling.…”

Section: Hippo Signaling In Contextmentioning

confidence: 81%

Integrating developmental signals: a Hippo in the (path)way

2011

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The Hippo pathway, a signaling cascade that controls cell cycle progression, apoptosis and cell differentiation, has emerged as a fundamental regulator of many physiological and pathological processes. Recent studies have revealed a complex network of interactions directing Hippo pathway activity, and have connected this pathway with other key signaling pathways. Such crosstalk has uncovered novel roles for Hippo signaling, including regulation of TGFb/SMAD and WNT/b-catenin pathways. This review highlights some of the recent findings in the Hippo field with an emphasis on how the Hippo pathway is integrated with other pathways to mediate diverse processes.

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Section: Hippo Signaling In Contextmentioning

confidence: 81%

Integrating developmental signals: a Hippo in the (path)way

2011

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“…STRAP recruits Smad7 to activated T␤R-I and stabilizes the Smad7-T␤R-I association, preventing R-Smad phosphorylation by T␤R-I and subsequent intracellular signaling. A recently identified Smad7-interacting protein, Yes-associated protein YAP65, functions as an inhibitor of TGF-␤ signaling in a manner similar to that of STRAP (44).…”

Section: Fig 3 Piasy Inhibits Tgf-␤-mediated Transcriptionmentioning

confidence: 99%

Regulation of Transforming Growth Factor-β Signaling by Protein Inhibitor of Activated STAT, PIASy through Smad3

Imoto

Sugiyama

Muromoto

et al. 2003

Journal of Biological Chemistry

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Smads proteins play a key role in the intracellular signaling of the transforming growth factor (TGF)-␤ family of growth factors, which exhibits a diverse set of cellular responses, including cell proliferation and differentiation. In particular, Smad7 acts as an antagonist of TGF-␤ signaling, which could determine the intensity or duration of its signaling cascade. In this study we identified a protein inhibitor of activated STAT (signal transducers and activators of transcription), PIASy, as a novel interaction partner of Smad7 by yeast two-hybrid screening using the MH2 domain of Smad7 as bait. The association of Smad7 and PIASy was confirmed using co-expressed tagged proteins in 293T cells. Moreover, we found that other Smads including Smad3 also associated with PIASy through its MH2 domain, and PIASy suppressed TGF-␤-mediated activation of Smad3. PIASy also stimulated the sumoylation of Smad3 in vivo. Furthermore, endogenous PIASy expression was induced by TGF-␤ in Hep3B cells. These findings provide the first evidence that a PIAS family protein, PIASy, associates with Smads and involves the regulation of TGF-␤ signaling using the negative feedback loop.

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“…STRAP thus affects TGF-b signaling via several mechanisms. Similarly, Yes-associated protein (YAP65) forms complexes with TbRI and enhances recruitment of Smad7 via direct interaction, leading to signaling downregulation (Ferrigno et al 2002). …”

Section: Signaling Via Tgf-b Receptors Is Modulated By Interactions Wmentioning

confidence: 99%

Signaling Receptors for TGF-β Family Members

Heldin

Moustakas

2016

Cold Spring Harb Perspect Biol

557

498

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Transforming growth factor b (TGF-b) family members signal via heterotetrameric complexes of type I and type II dual specificity kinase receptors. The activation and stability of the receptors are controlled by posttranslational modifications, such as phosphorylation, ubiquitylation, sumoylation, and neddylation, as well as by interaction with other proteins at the cell surface and in the cytoplasm. Activation of TGF-b receptors induces signaling via formation of Smad complexes that are translocated to the nucleus where they act as transcription factors, as well as via non-Smad pathways, including the Erk1/2, JNK and p38 MAP kinase pathways, and the Src tyrosine kinase, phosphatidylinositol 3 0 -kinase, and Rho GTPases.

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Yes-associated protein (YAP65) interacts with Smad7 and potentiates its inhibitory activity against TGF-β/Smad signaling

Cited by 201 publications

References 23 publications

Integrating developmental signals: a Hippo in the (path)way

Integrating developmental signals: a Hippo in the (path)way

Regulation of Transforming Growth Factor-β Signaling by Protein Inhibitor of Activated STAT, PIASy through Smad3

Signaling Receptors for TGF-β Family Members

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