Supplementary Materials
The SCFβ-TRCP E3 ubiquitin ligase complex targets Lipin1 for ubiquitination and degradation to promote hepatic lipogenesis
Kouhei Shimizu, Hidefumi Fukushima, Kohei Ogura, Evan C. Lien, Naoe Taira Nihira, Jinfang Zhang, Brian J. North, Ailan Guo, Katsuyuki Nagashima, Tadashi Nakagawa, Seira Hoshikawa, Asami Watahiki, Koji Okabe, Aya Yamada, Alex Toker, John M. Asara, Satoshi Fukumoto, Keiichi I. Nakayama, Keiko Nakayama, Hiroyuki Inuzuka,* Wenyi Wei*
*Corresponding author. Email: hinuzuka{at}bidmc.harvard.edu (H.I.); wwei2{at}bidmc.harvard.edu (W.W.)
This PDF file includes:
- Fig. S1. Validation of anti–β-TRCP phosphodegron antibodies.
- Fig. S2. Validation of β-TRCP substrates.
- Fig. S3. SCFβ-TRCP E3 ligase complex associates with Lipin1 to control its stability.
- Fig. S4. CKI phosphorylates the β-TRCP degron motif in Lipin1 to govern its ubiquitination and degradation by SCFβ-TRCP E3 ligase complex.
- Fig. S5. β-TRCP promotes SREBP transcriptional activity in part by triggering the ubiquitination and subsequent degradation of Lipin1.
- Fig. S6. β-TRCP controls lipogenesis in a Lipin1-dependent manner in hepatocytes.
- Fig. S7. A detailed schematic diagram of Lipin1 constructs used in this study.
- Fig. S8. β-TRCP1−/− mice are less insulin-resistant.
- Table S1. A list of candidate β-TRCP ubiquitin substrates identified with a phosphodegron antibody–mediated mass spectrometry approach.
- Table S2. Primers for real-time RT-PCR.
Technical Details
Format: Adobe Acrobat PDF
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Citation: K. Shimizu, H. Fukushima, K. Ogura, E. C. Lien, N. T. Nihira, J. Zhang, B. J. North, A. Guo, K. Nagashima, T. Nakagawa, S. Hoshikawa, A. Watahiki, K. Okabe, A. Yamada, A. Toker, J. M. Asara, S. Fukumoto, K. I. Nakayama, K. Nakayama, H. Inuzuka, W. Wei, The SCFβ-TRCP E3 ubiquitin ligase complex targets Lipin1 for ubiquitination and degradation to promote hepatic lipogenesis. Sci. Signal. 10, eaah4117 (2017).
