Acetylation Stabilizes ATP-Citrate Lyase to Promote Lipid Biosynthesis and Tumor Growth

• Published in: Molecular cell Vol. 51; no. 4; pp. 506 - 518
• Main Authors: Lin, Ruiting, Tao, Ren, Gao, Xue, Li, Tingting, Zhou, Xin, Guan, Kun-Liang, Xiong, Yue, Lei, Qun-Ying
• Format: Journal Article
• Language: English
• Published: United States Elsevier Inc 22.08.2013
• Subjects: Acetylation; Animals; ATP Citrate (pro-S)-Lyase - chemistry; ATP Citrate (pro-S)-Lyase - genetics; ATP Citrate (pro-S)-Lyase - metabolism; biosynthesis; Blotting, Western; Calmodulin-Binding Proteins - genetics; Calmodulin-Binding Proteins - metabolism; cell growth; Cell Proliferation; Cytoskeletal Proteins - genetics; Cytoskeletal Proteins - metabolism; fatty acids; Fatty Acids - metabolism; glucose; Humans; Immunoenzyme Techniques; lung neoplasms; Lung Neoplasms - genetics; Lung Neoplasms - metabolism; Lung Neoplasms - pathology; lysine; Male; Mice; Mice, Nude; neoplasm cells; p300-CBP Transcription Factors - genetics; p300-CBP Transcription Factors - metabolism; Proteasome Endopeptidase Complex - metabolism; Protein Processing, Post-Translational; Real-Time Polymerase Chain Reaction; Reverse Transcriptase Polymerase Chain Reaction; RNA, Messenger - genetics; Sirtuin 2 - genetics; Sirtuin 2 - metabolism; Tumor Cells, Cultured; Ubiquitin - metabolism; Ubiquitination

Increased fatty acid synthesis is required to meet the demand for membrane expansion of rapidly growing cells. ATP-citrate lyase (ACLY) is upregulated or activated in several types of cancer, and inhibition of ACLY arrests proliferation of cancer cells. Here we show that ACLY is acetylated at lysine...