SKP2- and OTUD1-regulated non-proteolytic ubiquitination of YAP promotes YAP nuclear localization and activity

• Published in: Nature communications Vol. 9; no. 1; pp. 2269 - 16
• Main Authors: Yao, Fan, Zhou, Zhicheng, Kim, Jongchan, Hang, Qinglei, Xiao, Zhenna, Ton, Baochau N., Chang, Liang, Liu, Na, Zeng, Liyong, Wang, Wenqi, Wang, Yumeng, Zhang, Peijing, Hu, Xiaoyu, Su, Xiaohua, Liang, Han, Sun, Yutong, Ma, Li
• Format: Journal Article
• Language: English
• Published: London Nature Publishing Group UK 11.06.2018; Nature Publishing Group; Nature Portfolio
• Subjects: 38/109; 42/89; 631/45/612/1254; 631/80/2023/2022; 631/80/458/582; 64/60; 82/29; 82/83; 96/95; Activation; Active Transport, Cell Nucleus; Adaptor Proteins, Signal Transducing - chemistry; Adaptor Proteins, Signal Transducing - genetics; Adaptor Proteins, Signal Transducing - metabolism; Amino Acid Substitution; Animals; Binding Sites - genetics; Cancer; Cell Line; Cell Nucleus - metabolism; Cytoplasm; Deactivation; DNA-Binding Proteins - metabolism; Female; Gene Knockout Techniques; HEK293 Cells; Humanities and Social Sciences; Humans; Inactivation; Localization; Mice; multidisciplinary; Mutagenesis, Site-Directed; Nuclear Proteins - metabolism; Phosphoproteins - chemistry; Phosphoproteins - genetics; Phosphoproteins - metabolism; Phosphorylation; Protein-Serine-Threonine Kinases - metabolism; Proteolysis; S-Phase Kinase-Associated Proteins - metabolism; Science; Science (multidisciplinary); Skp2 protein; Transcription; Transcription Factors - metabolism; Ubiquitin-protein ligase; Ubiquitin-Specific Proteases - metabolism; Ubiquitination; Yes-associated protein

Dysregulation of YAP localization and activity is associated with pathological conditions such as cancer. Although activation of the Hippo phosphorylation cascade is known to cause cytoplasmic retention and inactivation of YAP, emerging evidence suggests that YAP can be regulated in a Hippo-independ...