Autopalmitoylation of TEAD proteins regulates transcriptional output of the Hippo pathway

Chan, PuiYee; Han, Xiao; Zheng, Baohui; DeRan, Michael; Yu, Jianzhong; Jarugumilli, Gopala K.; Deng, Hua; Pan, Duojia; Luo, Xuelian; Wu, Xu

doi:10.1038/nchembio.2036

Title: Autopalmitoylation of TEAD proteins regulates transcriptional output of the Hippo pathway

Journal Article · Mon Feb 22 00:00:00 EST 2016 · Nature Chemical Biology

DOI:https://doi.org/10.1038/nchembio.2036· OSTI ID:1248393

Chan, PuiYee ^[1]; Han, Xiao ^[2]; Zheng, Baohui ^[1]; DeRan, Michael ^[1]; Yu, Jianzhong ^[3]; Jarugumilli, Gopala K. ^[1]; Deng, Hua ^[3]; Pan, Duojia ^[3]; Luo, Xuelian ^[4]; Wu, Xu ^[1]

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)

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.

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Research Organization:: Argonne National Laboratory (ANL), Argonne, IL (United States)

Sponsoring Organization:: 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.

Grant/Contract Number:: AC02-06CH11357; 24929-RSG-13-291-01-TBE; R01CA181537; R01DK107651-01; R01GM107415; R01EY015708

OSTI ID:: 1248393

Journal Information:: Nature Chemical Biology, Vol. 12, Issue 4; ISSN 1552-4450

Publisher:: Nature Publishing GroupCopyright Statement

Country of Publication:: United States

Language:: ENGLISH

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Cited by: 161 works

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