AMOTL2 interaction with TAZ causes the inhibition of surfactant proteins expression in lung cells. (Articolo in rivista)

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  • AMOTL2 interaction with TAZ causes the inhibition of surfactant proteins expression in lung cells. (Articolo in rivista) (literal)
Anno
  • 2013-01-01T00:00:00+01:00 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#doi
  • 10.1016/j.gene.2013.07.015. (literal)
Alternative label
  • Lucci V, Di Palma T, D'Ambrosio C, Scaloni A, Zannini M. (2013)
    AMOTL2 interaction with TAZ causes the inhibition of surfactant proteins expression in lung cells.
    in Gene (Amst.); Elsevier, Amsterdam (Paesi Bassi)
    (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori
  • Lucci V, Di Palma T, D'Ambrosio C, Scaloni A, Zannini M. (literal)
Pagina inizio
  • 300 (literal)
Pagina fine
  • 306 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#url
  • http://www.sciencedirect.com/science/article/pii/S0378111913008846 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroVolume
  • 529(): (literal)
Rivista
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#pagineTotali
  • 7 (literal)
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  • 2 (literal)
Note
  • PubMe (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni
  • CNR -- National Research Council, Institute of Experimental Endocrinology and Oncology (IEOS), Naples, Italy CNR -- National Research Council, Proteomics and Mass Spectrometry Laboratory (ISPAAM), Naples, Italy (literal)
Titolo
  • AMOTL2 interaction with TAZ causes the inhibition of surfactant proteins expression in lung cells. (literal)
Abstract
  • BACKGROUND: TAZ (Transcriptional co-Activator with PDZ-binding motif), is a biologically potent transcriptional coactivator and functions by binding to the PPXY motif present in several transcription factors. Notably, TAZ behaves as a transducer linking cytoplasmic signaling events to transcriptional regulation in the nucleus. Several different factors regulate TAZ expression and/or function. In particular, a major regulation of TAZ activity occurs through the Hippo pathway by a phosphorylation-mediated mechanism that causes its cytoplasmic sequestration or degradation. RESULTS: Here we demonstrate that AMOTL2 robustly co-immunoprecipitates with TAZ, and their interaction is dependent on the WW domain of TAZ and the PPXY motif in the N-terminus of AMOTL2. Furthermore, we show that AMOTL2 colocalizes with TAZ in the cytoplasm of H441 human lung cells and regulates TAZ cytoplasm-to-nucleus translocation through direct protein-protein interaction. Interestingly, the overexpression of AMOTL2 inhibits the functional cooperation between the transcription factor TTF-1 and TAZ on the Surfactant C gene promoter, as well as the expression of other known target genes of these regulatory factors. CONCLUSIONS: Taken together, our results suggest an inhibitory role of AMOTL2 on TAZ ability to co-activate transcription and describe a different mechanism, Hippo pathway-independent, that modulates the activity of TAZ in lung cells through the interaction with Angiomotin-like 2 (AMOTL2). (literal)
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