Autopalmitoylation of TEAD proteins regulates transcriptional output of the Hippo pathway
Abstract
TEA domain (TEAD) transcription factors bind to the coactivators YAP and TAZ and regulate the transcriptional output of the Hippo pathway, playing critical roles in organ size control and tumorigenesis. Protein S-palmitoylation attaches a fatty acid, palmitate, to cysteine residues and regulates protein trafficking, membrane localization and signaling activities. Using activity-based chemical probes, we discovered that human TEADs possess intrinsic palmitoylating enzyme–like activities and undergo autopalmitoylation at evolutionarily conserved cysteine residues under physiological conditions. We determined the crystal structures of lipid-bound TEADs and found that the lipid chain of palmitate inserts into a conserved deep hydrophobic pocket. Strikingly, palmitoylation did not alter TEAD's localization, but it was required for TEAD's binding to YAP and TAZ and was dispensable for its binding to the Vgll4 tumor suppressor. Moreover, palmitoylation-deficient TEAD mutants impaired TAZ-mediated muscle differentiation in vitro and tissue overgrowth mediated by the Drosophila YAP homolog Yorkie in vivo. Furthermore, our study directly links autopalmitoylation to the transcriptional regulation of the Hippo pathway.
- Authors:
-
- Harvard Medical School, Charlestown, MA (United States)
- Jilin Univ., Changchun (China); Univ. of Texas Southwestern Medical Center, Dallas, TX (United States)
- Johns Hopkins Univ. School of Medicine, Baltimore, MD (United States)
- Univ. of Texas Southwestern Medical Center, Dallas, TX (United States)
- Publication Date:
- Research Org.:
- Argonne National Laboratory (ANL), Argonne, IL (United States)
- Sponsoring Org.:
- USDOE; American Cancer Society; U.S. National Inst. of Health/National Cancer Inst.; National Inst. of Health/National Inst. of Diabetes and Digestive and Kidney Diseases; National Inst. of Health/National Inst. of General Medical Sciences; National Inst. of Health/National Eye Inst.
- OSTI Identifier:
- 1248393
- Grant/Contract Number:
- AC02-06CH11357; 24929-RSG-13-291-01-TBE; R01CA181537; R01DK107651-01; R01GM107415; R01EY015708
- Resource Type:
- Journal Article: Accepted Manuscript
- Journal Name:
- Nature Chemical Biology
- Additional Journal Information:
- Journal Volume: 12; Journal Issue: 4; Journal ID: ISSN 1552-4450
- Publisher:
- Nature Publishing Group
- Country of Publication:
- United States
- Language:
- ENGLISH
- Subject:
- 59 BASIC BIOLOGICAL SCIENCES; Cell signalling; Drosophilia; Post-translational modifications; X-ray crystallography
Citation Formats
Chan, PuiYee, Han, Xiao, Zheng, Baohui, DeRan, Michael, Yu, Jianzhong, Jarugumilli, Gopala K., Deng, Hua, Pan, Duojia, Luo, Xuelian, and Wu, Xu. Autopalmitoylation of TEAD proteins regulates transcriptional output of the Hippo pathway. United States: N. p., 2016.
Web. doi:10.1038/nchembio.2036.
Chan, PuiYee, Han, Xiao, Zheng, Baohui, DeRan, Michael, Yu, Jianzhong, Jarugumilli, Gopala K., Deng, Hua, Pan, Duojia, Luo, Xuelian, & Wu, Xu. Autopalmitoylation of TEAD proteins regulates transcriptional output of the Hippo pathway. United States. https://doi.org/10.1038/nchembio.2036
Chan, PuiYee, Han, Xiao, Zheng, Baohui, DeRan, Michael, Yu, Jianzhong, Jarugumilli, Gopala K., Deng, Hua, Pan, Duojia, Luo, Xuelian, and Wu, Xu. 2016.
"Autopalmitoylation of TEAD proteins regulates transcriptional output of the Hippo pathway". United States. https://doi.org/10.1038/nchembio.2036. https://www.osti.gov/servlets/purl/1248393.
@article{osti_1248393,
title = {Autopalmitoylation of TEAD proteins regulates transcriptional output of the Hippo pathway},
author = {Chan, PuiYee and Han, Xiao and Zheng, Baohui and DeRan, Michael and Yu, Jianzhong and Jarugumilli, Gopala K. and Deng, Hua and Pan, Duojia and Luo, Xuelian and Wu, Xu},
abstractNote = {TEA domain (TEAD) transcription factors bind to the coactivators YAP and TAZ and regulate the transcriptional output of the Hippo pathway, playing critical roles in organ size control and tumorigenesis. Protein S-palmitoylation attaches a fatty acid, palmitate, to cysteine residues and regulates protein trafficking, membrane localization and signaling activities. Using activity-based chemical probes, we discovered that human TEADs possess intrinsic palmitoylating enzyme–like activities and undergo autopalmitoylation at evolutionarily conserved cysteine residues under physiological conditions. We determined the crystal structures of lipid-bound TEADs and found that the lipid chain of palmitate inserts into a conserved deep hydrophobic pocket. Strikingly, palmitoylation did not alter TEAD's localization, but it was required for TEAD's binding to YAP and TAZ and was dispensable for its binding to the Vgll4 tumor suppressor. Moreover, palmitoylation-deficient TEAD mutants impaired TAZ-mediated muscle differentiation in vitro and tissue overgrowth mediated by the Drosophila YAP homolog Yorkie in vivo. Furthermore, our study directly links autopalmitoylation to the transcriptional regulation of the Hippo pathway.},
doi = {10.1038/nchembio.2036},
url = {https://www.osti.gov/biblio/1248393},
journal = {Nature Chemical Biology},
issn = {1552-4450},
number = 4,
volume = 12,
place = {United States},
year = {Mon Feb 22 00:00:00 EST 2016},
month = {Mon Feb 22 00:00:00 EST 2016}
}
Web of Science
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