T
Tingting Li
Researcher at Fudan University
Publications - 8
Citations - 1359
Tingting Li is an academic researcher from Fudan University. The author has contributed to research in topics: Acetylation & Hippo signaling pathway. The author has an hindex of 8, co-authored 8 publications receiving 1130 citations.
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Journal ArticleDOI
The Hippo Tumor Pathway Promotes TAZ Degradation by Phosphorylating a Phosphodegron and Recruiting the SCFβ-TrCP E3 Ligase *
Chen Ying Liu,Zhengyu Zha,Xin Zhou,Heng Zhang,Wei Huang,Di Zhao,Tingting Li,Siew Wee Chan,Chun Jye Lim,Wanjin Hong,Shimin Zhao,Yue Xiong,Yue Xiong,Qun-Ying Lei,Kun-Liang Guan,Kun-Liang Guan +15 more
TL;DR: It is reported here that TAZ protein stability is controlled by a phosphodegron recognized by the F-box protein β-TrCP and ubiquitylated by the SCF/CRL1β-Tr CP E3 ligase.
Journal ArticleDOI
Acetylation stabilizes ATP-citrate lyase to promote lipid biosynthesis and tumor growth
Ruiting Lin,Ren Tao,Xue Gao,Tingting Li,Xin Zhou,Kun-Liang Guan,Kun-Liang Guan,Yue Xiong,Yue Xiong,Qun-Ying Lei +9 more
TL;DR: A crosstalk between acetylation and ubiquitylation is revealed by competing for the same lysine residues in the regulation of fatty acid synthesis and cell growth in response to glucose.
Journal ArticleDOI
Mitogenic and oncogenic stimulation of K433 acetylation promotes PKM2 protein kinase activity and nuclear localization.
Lei Lv,Yan Ping Xu,Di Zhao,Fulong Li,Wei Wang,Naoya Sasaki,Ying Jiang,Xin Zhou,Xin Zhou,Tingting Li,Kun-Liang Guan,Qun-Ying Lei,Yue Xiong,Yue Xiong +13 more
TL;DR: K433 acetylation links cell proliferation and transformation to the switch of PKM2 from a cytoplasmic metabolite kinase to a nuclear protein kinase.
Journal ArticleDOI
PP1 Cooperates with ASPP2 to Dephosphorylate and Activate TAZ
Chen Ying Liu,Xianbo Lv,Tingting Li,Yanping Xu,Xin Zhou,Shimin Zhao,Yue Xiong,Yue Xiong,Qun-Ying Lei,Kun-Liang Guan,Kun-Liang Guan +10 more
TL;DR: PP1 as a bona fide TAZ phosphatase is identified and PP1A and ASPP2 play a critical role in promoting TAZ function by antagonizing the LATS kinase through TAZ dephosphorylation.
Journal ArticleDOI
Oxidative stress activates SIRT2 to deacetylate and stimulate phosphoglycerate mutase.
Yanping Xu,Fulong Li,Lei Lv,Tingting Li,Xin Zhou,Chu-Xia Deng,Kun-Liang Guan,Kun-Liang Guan,Qun Ying Lei Lei,Yue Xiong +9 more
TL;DR: It is reported that PGAM is acetylated at lysine 100 (K100), an active site residue that is invariably conserved from bacteria, to yeast, plant, and mammals and revealed a mechanism of PGAM2 regulation and NADPH homeostasis in response to oxidative stress that impacts cell proliferation and tumor growth.