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YAP1 Recruits c-Abl to Protect Angiomotin-Like 1 from Nedd4-Mediated Degradation
Stockholm University, Faculty of Science, The Wenner-Gren Institute , Developmental Biology.
2012 (English)In: PLoS ONE, ISSN 1932-6203, E-ISSN 1932-6203, Vol. 7, no 4, e35735- p.Article in journal (Refereed) Published
Abstract [en]

Background: 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. Methodology/Principal Findings: 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. Conclusions/Significance: 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.

Place, publisher, year, edition, pages
2012. Vol. 7, no 4, e35735- p.
National Category
Other Medical Biotechnology
Identifiers
URN: urn:nbn:se:su:diva-80758DOI: 10.1371/journal.pone.0035735ISI: 000305336000054OAI: oai:DiVA.org:su-80758DiVA: diva2:557803
Note

AuthorCount:2;

Available from: 2012-09-29 Created: 2012-09-27 Last updated: 2017-12-07Bibliographically approved

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