WW (WWP) Domains: From Structure to Function

Rotin, Daniela

doi:10.1007/978-3-642-80481-6_5

Cited by 32 publications

(40 citation statements)

References 70 publications

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“…Many of these interactions rely on the WW domain of TAZ/YAP (reviewed in Hong and Yaffe (2006);Sudol (2011)). The WW domain is a motif of B40 amino acid with conserved tryptophan and proline residues (Rotin, 1998). This domain recognizes proline-rich modules known as PY motifs found in various proteins (reviewed in Sudol et al (2001)).…”

Section: Hippo Signaling In Contextmentioning

confidence: 99%

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: 99%

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

2011

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“…Mutation of this conserved cysteine residue to an alanine (C710A) abolished the ubiquitination and degradation activity of Smurf1 (Zhu et al, 1999). Another motif often found in the Hect domain family of E3 ligase is the WW domain, which contains two highly conserved tryptophans and a conserved proline in an approximately 30-amino acid region (Rotin, 1998;Zhu et al, 1999). The WW domains have a preference for binding to small proline-rich sequences, PPXY motifs, and different WW domains possess different substrate specificity.…”

Section: Ubiquitin-proteasome Degradation Of Bmp Signaling Proteinsmentioning

confidence: 99%

The BMP signaling and in vivo bone formation

Cao

Chen

2005

Gene

273

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Bone morphogenetic proteins (BMPs) are multi-functional growth factors that belong to the transforming growth factor β(TGFβ) superfamily. The roles of BMPs in embryonic development and cellular functions in postnatal and adult animals have been extensively studied in recent years. Signal transduction studies have revealed that Smads 1, 5 and 8 are the immediate downstream molecules of BMP receptors and play a central role in BMP signal transduction. Studies from transgenic and knockout mice and from animals and humans with naturally occurring mutations in BMPs and their signaling molecules have shown that BMP signaling plays critical roles in bone and cartilage development and postnatal bone formation. BMP activities are regulated at different molecular levels. Tissue-specific knockout of a specific BMP ligand, a subtype of BMP receptors or a specific signaling molecule is required to further determine the specific role of a BMP ligand, receptor or signaling molecule in a particular tissue.

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“…PEPP1, PEPP2 and PEPP3 are poorly conserved in the region C-terminal to the PH domain ( Figure 6A). PEPP2, but not PEPP1 or PEPP3, also possesses two WW domains [29] in a region Nterminal to the PH domain ( Figure 6A). PEPP2 might be more widely expressed than PEPP1, since Northern blot analysis shows that PEPP2 mRNA is present in high levels in heart and kidney, and is also expressed at a lower level in other tissues.…”

Section: Plant Atph1 and Mammalian Pepp1 Bind Ptdins3p Specificallymentioning

confidence: 99%