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Medical AI Inquiry: You was designed to assist in medical decision-making based on the provided user questions. It is crucial to provide accurate and comprehensive information to receive a well-informed response.  Labels: BACKGROUND, RESULTS. Meshes: Adaptor Proteins, Signal Transducing, Amino Acid Sequence, Animals, Cell Line, Dogs, Endosomal Sorting Complexes Required for Transport, Epithelial Cells, Gene Expression, Humans, Membrane Proteins, Molecular Sequence Data, Nedd4 Ubiquitin Protein Ligases, Phosphoproteins, Phosphorylation, Proteasome Endopeptidase Complex, Proteolysis, Proto-Oncogene Proteins c-abl, RNA, Small Interfering, Signal Transduction, Tight Junctions, Transfection, Ubiquitin, Ubiquitin-Protein Ligases, Ubiquitination.
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Does yAP1 recruit c-Abl to protect angiomotin-like 1 from Nedd4-mediated degradation? Context: Tissue development and organ growth require constant remodeling of cell-cell contacts formed between epithelial cells. The Hippo signaling cascade curtails organ growth by excluding the transcriptional co-activator Yes Associated Protein 1 (YAP1) from the nucleus. Angiomotin family members recruit YAP1 to tight junctions [1], but whether YAP1 plays a specific role outside of the nucleus is currently unknown. The present study demonstrates that the E3 ubiquitin ligase Nedd4.2 targets Angiomotin-like 1 (AMOTL1), a family member that promotes the formation of epithelial tight junctions, for ubiquitin-dependent degradation. Unexpectedly, YAP1 antagonizes the function of Nedd4.2, and protects AMOTL1 against Nedd4.2-mediated degradation. YAP1 recruits c-Abl, a tyrosine kinase that binds and phosphorylates Nedd4.2 on tyrosine residues, thereby modifying its ubiquitin-ligase activity.
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Our results uncover a novel function for cytoplasmic YAP1. YAP1 recruits c-Abl to protect AMOTL1 against Nedd4.2-mediated degradation. Thus, YAP1, excluded from the nucleus, contributes to the maintenance of tight junctions. Final Decision: yes