http://www.cnr.it/ontology/cnr/individuo/prodotto/ID252608
AMOTL2 interaction with TAZ causes the inhibition of surfactant proteins expression in lung cells. (Articolo in rivista)
- Type
- Label
- 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)
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- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori
- Lucci V, Di Palma T, D'Ambrosio C, Scaloni A, Zannini M. (literal)
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- http://www.sciencedirect.com/science/article/pii/S0378111913008846 (literal)
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- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroFascicolo
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- 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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