CTCP Tập đoàn Nova Consumer (mã NCG) vừa công bố đơn từ nhiệm chức vụ thành viên HĐQT kiêm tổng giám đốc của ông Nguyễn Quang Phi Tín. Trong đơn, ông Tín cho biết nguyên nhân từ nhiệm là vì “lý do cá nhân”. Sau đơn từ nhiệm của ông Nguyễn Quang Phi Tín, HĐQT của Nova Consumer sẽ chỉ còn 2 thành viên, gồm Chủ tịch HĐQT Nguyễn Hiếu Liêm và Thành viên độc lập HĐQT Trần Thị Thu Thảo. ĐHĐCĐ bất thường năm 2025 của Nova Consumer dự kiến diễn ra ngày 27/8 tới đây sẽ thông qua đơn từ nhiệm của ông Tín và bầu bổ sung thành viên HĐQT. Ngày đăng ký cuối cùng là 30/7/2025. Ông Nguyễn Quang Phi Tín trở thành tổng giám đốc kiêm thành viên HĐQT của Nova Consumer từ tháng 3/2022, và kiêm nhiệm hai vị trí này cho đến nay. Bên cạnh vai trò tại công ty mẹ, theo báo cáo quản trị năm 2024 của NCG, ông Tín còn đảm nhận nhiều vị trí khác tại các công ty thành viên như thành viên HĐQT của CTCP Anova Farm, thành viên HĐQT của Anova Feed, tổng giám đốc của Công ty TNHH Sản xuất và Thương mại Nova Beverages…
Trong một diễn biến liên quan, trước đó vào ngày 19/6/2025, HĐQT Nova Consumer đã quyết định bổ nhiệm bà Đặng Ngọc Khánh Vân (SN 1980) vào vị trí phó tổng giám đốc điều hành và quản trị hệ thống. Bà Khánh Vân có trách nhiệm thiết lập và hận hành hệ thống chuẩn hóa toàn công ty và các công ty thành viên; điều hành hoạt động triển khai và giám sát quy trình thao tác chuẩn tại các phòng ban, đơn vị kinh doanh; dẫn dắt chương trình chuyển đổi số toàn hệ thống; trực tiếp quản lý ban hành chính – nhân sự, phòng quản lý quy trình và tuân thủ, phòng công nghệ thông tin. Trên sàn chứng khoán, cổ phiếu NCG đang dừng ở mức 9.600 đồng/cp, tăng 26% so với đầu năm. Vốn hóa thị trường tương ứng gần 1.150 tỷ đồng. Hà Linh

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Abstract
As an enzyme with a critical role in de novo purine synthesis, adenylosuccinate lyase (ADSL) expression is upregulated in various malignancies. However, whether ADSL possesses noncanonical functions that contribute to cancer progression remains poorly understood. Here, we demonstrate that protein kinase R-like endoplasmic reticulum kinase (PERK) activated by lipid deprivation or ER stress phosphorylates ADSL at S140, leading to an enhanced association between ADSL and Beclin1. Beclin1-associated ADSL produces fumarate, which in turn inhibits lysine demethylase 8-mediated Beclin1 demethylation, resulting in enhanced Beclin1 K117me2, subsequent disruption of the binding of BCL-2 to Beclin1 and elevated autophagy. Blocking the ADSL–Beclin1 axis by knock-in mutation or a cell-penetrating peptide inhibits autophagy induced by lipid deprivation and ER stress and blunts liver tumor growth in mice. Additionally, ADSL pS140-upregulated Beclin1 K117me2 levels are positively correlated with autophagy levels in human hepatocellular carcinoma specimens and poor patient prognosis. These findings uncover the function of ADSL in autophagy regulation and liver tumor development. Access options
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Fig. 2: PERK-mediated ADSL S140 phosphorylation promotes autophagy. Fig. 3: ADSL inhibits Beclin1 demethylation and its binding to BCL-2. Fig. 4: ADSL-mediated Beclin1 K117me2 promotes autophagy. Fig. 5: ADSL-mediated Beclin1 K117me2 promotes liver tumor growth. Fig. 6: The ADSL–Beclin1 axis is related to HCC clinical aggressiveness. Data availability
The data that support the findings of this study are available in the main text and Supplementary Information . All other data supporting the findings of this study are available from the corresponding author on reasonable request. The UniProt protein database (EMBL-EBI) was used for protein identification. The X-ray crystal structure of KDM8 (JMJD5) was derived from the PDB under accession code 6F4O . Gene IDs were determined from the NCBI ( http://www.ncbi.nlm.nih.gov/gene ). MS data were deposited to ProteomeXchange under accession code PXD057286 . Source data are provided with this paper. References
White, E. Deconvoluting the context-dependent role for autophagy in cancer. Nat. Rev. Cancer 12, 401–410 (2012). Yang, W. et al. Nuclear PKM2 regulates β-catenin transactivation upon EGFR activation. Nature 480, 118–122 (2011). Acknowledgements
This study was supported by grants from the National Natural Science Foundation of China (82188102 and 82030074, to Z.L. ; 32470815, 92157113 and 82072630, to D.X. ; 82372814 and 82173114, to Z.W. ), the Ministry of Science and Technology of the People’s Republic of China (2021YFA0805600, to D.X. ; 2020YFA0803300, to Z.L. ; 2023YFC2606500, to P.Z. ), the Zhejiang Natural Science Foundation Key Project (LD22H160002, to D.X. ; LD21H160003, to Z.L. ), the Zhejiang Natural Science Foundation Discovery Project (LQ22H160023, to Z.W.) and the Zhejiang University Research Fund (188020*194221901/029, to Z.L.). Z.L. is the Kuancheng Wang Distinguished Chair. The author gratefully acknowledges the support of the K.C. Wong Education Foundation. Author information
Authors and Affiliations
Zhejiang Provincial Key Laboratory of Pancreatic Disease, The First Affiliated Hospital, Institute of Translational Medicine, Zhejiang University School of Medicine, Zhejiang University, Hangzhou, China
Lei Wang, Yuran Duan, Zheng Wang, Peixiang Zheng, Guimei Ji, Yuli Shen, Bofei Dong, Yanni Lin, Ting Wen, Qi Tian, Zhanpeng Guo, Yueru Hou, Shiqi Wu, Ling Xiao, Min Li, Liwei Xiao, Qingang Wu, Ying Meng, Guijun Liu, Xueli Bai, Zhimin Lu & Daqian Xu
Zhejiang Key Laboratory of Frontier Medical Research on Cancer Metabolism, Hangzhou, China
Lei Wang, Yuran Duan, Zheng Wang, Peixiang Zheng, Guimei Ji, Yuli Shen, Bofei Dong, Yanni Lin, Ting Wen, Qi Tian, Zhanpeng Guo, Yueru Hou, Shiqi Wu, Ling Xiao, Min Li, Liwei Xiao, Qingang Wu, Ying Meng, Guijun Liu, Zhimin Lu & Daqian Xu
Institute of Fundamental and Transdisciplinary Research, Cancer Center, Zhejiang University, Hangzhou, China
Lei Wang, Yuran Duan, Zheng Wang, Zhimin Lu & Daqian Xu
Department of Surgical Oncology, Harbin Medical University Cancer Hospital, Harbin, China
Runze Shi, Xue Sun, Xiaohan Chen & Tong Liu
Department of Medicinal Chemistry, Key Laboratory of Chemical Biology, Ministry of Education, School of Pharmaceutical Sciences, Shandong University, Jinan, China
Shuo Wang & Peng Zhan
Sofie Duan
Tong Liu, Zhiren Zhang & Daqian Xu
Departments of Cardiology and Critical Care Medicine, The First Affiliated Hospital of Harbin Medical University, Key Laboratories of Education Ministry for Myocardial Ischemia Mechanism and Treatment, Harbin, China
Zhiren Zhang
Runze Shi
Shuo Wang
Yuran Duan
Zheng Wang
Peixiang Zheng
Xue Sun
Xiaohan Chen
Guimei Ji
Yuli Shen
Bofei Dong
Yanni Lin
Ting Wen
Qi Tian
Zhanpeng Guo
Yueru Hou
Shiqi Wu
Ling Xiao
Min Li
Liwei Xiao
Qingang Wu
Ying Meng
Guijun Liu
Sofie Duan
Xueli Bai
Tong Liu
Zhiren Zhang
Peng Zhan
Zhimin Lu
Daqian Xu
Contributions
D.X. conceptualized and designed the study and wrote the manuscript. D.X., Z.L. and P.Z. acquired the funding and supervised the study. L.W., R.S., Z.W. and Y.D. designed most of the experiments, performed most of the experiments (including cell biology and biochemical experiments and animal studies), analyzed most of the data and wrote the manuscript. P.Z., X.S., X.C. and G.J. performed the experiments and analyzed the western blot and qPCR data. Y.S., B.D., Y.L. and T.W. performed the experiments and conducted the immunofluorescence analysis. Q.T., Z.G., M.L., L.X., Q.W. and Y.M. performed the experiments and conducted the IHC analysis. S.W. and P.Z. were involved in MD simulation analyses. Y.H., S.W., L.X., G.L. and S.D. performed statistical analysis and interpretation of the data. X.B. and T.L. reviewed and edited the manuscript. Z.Z. provided technical support. Corresponding author
Peer review
Peer review information
Nature Chemical Biology thanks Marco Sciacovelli, Qing Zhang and the other, anonymous reviewer(s) for their contribution to the peer review of this work. Additional information
Publisher’s note Springer Nature remains neutral with regard to jurisdictional claims in published maps and institutional affiliations. Extended data
a-e,g-j, Immunoprecipitation and immunoblotting analyses with the indicated antibodies were performed; representative results from three independent experiments are shown. a, Huh7 cells transfected with Flag-Beclin1 were cultured with or without lipids (LD), amino acids (AA), or glucose (Glc) for the indicated times. The band intensities were quantified. Data represent the mean ± SD from 3 independent experiments. b, Huh7 cells were pretreated with or without Compound C (5 μM), SP600125 (20 μM), SB203580 (10 μM), or GSK2656157 (10 μM) for 30 min before treated with or without LD for 4 h. c, A GST pull-down assay was performed by mixing purified PERK with purified GST, GST-ADSL, or GST-Beclin1. d,e, Huh7 cells transfected with the indicated plasmids were treated with or without LD for 4 h. f, Flag-streptavidin-PERK WT and K622A purified from Huh7 cells were analyzed by SDS-PAGE. g,h, Purified active GST-PERK (563-1115) was incubated with or without the indicated purified His-ADSL (g) or purified Flag/strep-PERK was incubated with or without the indicated purified GST-ADSL or GST-Beclin1 (h) in the presence of [γ-32P] ATP. i, Huh7 cells with ADSL depletion and reconstituted expression of the indicated shRNA-resistant Flag-rADSL proteins were treated with or without LD for 4 h. j, MEFs with or without PERK knockout were treated with or without LD for 4 h.
a,b,d,e, Huh7 cells stably transfected with the indicated plasmids were treated with or without 5 µg/mL TM for 4 h. Representative images of GFP-WIPI2 (a,d) or GFP-LC3 (b,e) puncta are shown (top). The numbers of WIPI2 or LC3 puncta in 50 cells were quantitated in each experiment (bottom). Data represent the mean ± s.d. from 3 independent experiments (two-way ANOVA). c,f, Huh7 cells with ADSL depletion and reconstituted expression of the indicated shRNA-resistant Flag-rADSL proteins were treated with or without 5 µg/mL TM in the presence or absence of 100 nM bafilomycin A1 for 4 h. Immunoblotting analyses with the indicated antibodies were performed; representative results from three independent experiments are shown. a-h, Immunoprecipitation and immunoblotting analyses with the indicated antibodies were performed; representative results from three independent experiments are shown. a,b, Huh7 (a,b) or HCCLM3 (b) cells with ADSL depletion and reconstituted expression of the indicated shRNA-resistant Flag-rADSL proteins or were treated with or without LD for 4 h. c, Huh7 cells were pretreated with or without 500 µM DFO (top) or 200 μM IOX1 (bottom) for 12 h, followed by treatment with or without LD for 4 h. d, The total cell lysates of Huh7 cells transfected with the indicated plasmids were harvested. e, Huh7 cells with KDM8 depletion and reconstituted expression of the indicated shRNA-resistant Flag-rKDM8 proteins were treated with or without 5 µg/mL TM for 4 h. f, Huh7 cells with Beclin1 depletion and reconstituted expression of the indicated shRNA-resistant Flag-rBeclin1 proteins were treated with or without 5 µg/mL TM for 4 h. g, Huh7 cells with ADSL depletion and reconstituted expression of the indicated shRNA-resistant Flag-rADSL proteins were stably transfected with KDM8 shRNA and treated with or without 5 µg/mL TM for 4 h. h, Huh7 cells with ADSL depletion and reconstituted expression of the indicated shRNA-resistant Flag-rADSL proteins were harvested. d,f, Immunoblotting analyses with the indicated antibodies were performed; representative results from three independent experiments are shown. a, Huh7 (top) and HCCLM3 (bottom) cells with or without Beclin1 depletion and reconstituted expression of the indicated shRNA-resistant Flag-rBeclin1 proteins were treated with or without 5 µg/mL TM for 4 h. The relative PI(3)P level was measured. Data represent the mean ± s.d. from 6 independent experiments (two-way ANOVA). b,c, Huh7 cells stably transfected with the indicated plasmids were treated with or without 5 µg/mL TM for 4 h. Representative images of GFP-WIPI2 (b) or GFP-LC3 puncta (c) are shown (top). The numbers of WIPI2 or LC3 puncta were quantitated (bottom). Data represent the mean ± s.d. from 3 independent experiments (two-way ANOVA). d, Huh7 cells with Beclin1 depletion and reconstituted expression of the indicated shRNA-resistant Flag-rBeclin1 proteins were treated with or without 5 µg/mL TM in the presence or absence of 100 nM bafilomycin A1 for 4 h. e, Huh7 cells stably transfected with the indicated plasmids were treated with or without LD for 4 h. Representative images of GFP-WIPI2 or GFP-LC3 puncta are shown (top). The numbers of WIPI2 or LC3 puncta were quantitated (bottom). Data represent the mean ± s.d. from 3 independent experiments (two-tailed Student’s t-test). f, Huh7 and HCCLM3 cells with ADSL depletion and reconstituted expression of the indicated shRNA-resistant Flag-rADSL proteins were stably transfected with KDM8 shRNA and treated with or without LD for 4 h.
e,f, Immunoblotting analyses with the indicated antibodies were performed; representative results from three independent experiments are shown. a, Evolution of the backbone root-mean-square-deviation (RMSD) of the KDM8-α-KG complex (top) or KDM8-fumarate complex (bottom) from the initial frame in 250 ns MD simulations. b, ITC assays were used to test the binding affinity of α-KG (800 nM) (top) or fumarate (800 nM) (bottom) to recombinant WT KDM8 (0.05 mM) or KDM8 Q275A (0.05 mM). c,d, BLI was used to test the interaction of α-KG (c) or fumarate (d) to recombinant WT KDM8 (top) or KDM8 Q275A (bottom). Sensors were loaded with biotinylated WT KDM8 or KDM8 Q275A. e, The total lysate of Huh7 cells with KDM8 depletion and reconstituted expression of the indicated shRNA-resistant Flag-rKDM8 proteins were stably transfected with HA-rADSL proteins were harvested. f, Huh7 cells with KDM8 depletion and reconstituted expression of the indicated shRNA-resistant Flag-rKDM8 proteins were stably transfected with HA-rADSL proteins were treated with or without LD for 4 h.
a-f, Immunoblotting analyses with the indicated antibodies were performed; representative results from three independent experiments are shown. a, Huh7 cells with or without Beclin1 depletion and reconstituted expression of the indicated shRNA-resistant Flag-rBeclin1 proteins were harvested. b,c, Huh7 cells with Beclin1 depletion and reconstituted expression of the indicated shRNA-resistant Flag-rBeclin1 proteins were treated with or without LD for 4 h (b) or 5 µg/mL TM for 4 h (c). d, Huh7 cells with or without ADSL depletion and reconstituted expression of the indicated shRNA-resistant HA-rADSL proteins were harvested. e,f, Huh7 cells with Beclin1 depletion and reconstituted expression of the indicated shRNA-resistant Flag-rBeclin1 proteins were stably transfected with HA-rADSL proteins and were treated with or without LD for 4 h (e) or 5 µg/mL TM for 4 h (f). a, Huh7 cells with Beclin1 depletion and reconstituted expression of the indicated shRNA-resistant Flag-rBeclin1 proteins were cultured in lipid depletion for 4 h. Representative images of GFP-WIPI2 or GFP-LC3 puncta are shown (top). The numbers of WIPI2 or LC3 puncta in 50 cells were quantitated in each experiment (bottom). Data represent the mean ± s.d. from 3 independent experiments (two-tailed Student’s t-test). b, Huh7 cells with Beclin1 depletion and reconstituted expression of the indicated shRNA-resistant Flag-rBeclin1 proteins were cultured in lipid depletion for 4 h. Immunoblotting analyses with the indicated antibodies were performed; representative results from three independent experiments are shown. a-f, Parental Huh7 cells (1 × 106) and the indicated clones with ADSL S140A (a) and Beclin1 K117R (c) knock-in expression were intrahepatically injected into 6-week-old male athymic BALB/c nude mice (n = 6 per group). Liver tumor growth was examined 28 days after injection (top). The arrows indicate tumors. Tumor volumes were calculated (bottom). Data represent the mean ± s.d. (one-way ANOVA). (b,d) IHC analyses of the indicated xenograft tumors from nude mice (n = 6) were performed. Representative staining images are shown. (e) IHC analyses of the indicated tumor samples were performed with an anti-Ki67 antibody (top). Ki67-positive cells were quantified (bottom) and quantification was averaged from the mean of each experiment. Data represent the mean ± s.d. (n = 6) (one-way ANOVA). (f) TUNEL analyses of the indicated tumor samples were performed (top). Apoptotic cells were stained brown and quantified (bottom) and quantification was averaged from the mean of each experiment. Data represent the mean ± s.d. (n = 6) (one-way ANOVA). g-l, Parental Huh7 cells (1 × 106) as well as the indicated clones with knock-in expression of ADSL S140A (g-i) or Beclin1 K117R (j-l) mutants were subcutaneously injected into 6-week-old male athymic BALB/c nude mice (n = 6 per group). The resulting tumors were resected 28 days after injection (g,j). The growth of xenografted tumors in the mice was measured (h,k). Data represent the mean ± s.d. (two-way ANOVA). The tumors were weighed (i,l). Data represent the mean ± s.d. (one-way ANOVA). a, Huh7 cells with ADSL depletion and reconstituted expression of the indicated shRNA-resistant Flag-rADSL proteins were stably transfected with ATG7 shRNA and treated with or without LD (left) or 5 µg/mL TM (right) for 48 h. Immunoblotting analyses with the indicated antibodies were performed; representative results from three independent experiments are shown. b, Huh7 cells with ADSL depletion and reconstituted expression of the indicated shRNA-resistant Flag-rADSL proteins were stably transfected with ATG7 shRNA and treated with or without LD (top) or 5 µg/mL TM (bottom), and then apoptosis was measured. Data represent the mean ± s.d. from 3 independent experiments (two-way ANOVA). c, Huh7 cells with ADSL depletion and reconstituted expression of the indicated shRNA-resistant Flag-rADSL proteins were stably transfected with ATG7 shRNA and treated with or without LD (left) or 5 µg/mL TM (right) for the indicated time, and then cell viability was measured. Data represent the mean ± s.d. from 3 independent experiments (two-way ANOVA). d-g, Huh7 cells (1 × 106) with ADSL depletion and reconstituted expression of the indicated shRNA-resistant Flag-rADSL proteins were stably transfected with ATG7 shRNA and subcutaneously injected into 6-week-old male athymic BALB/c nude mice (n = 6 per group). The resulting tumors were resected 22 days after injection (d). The growth of xenografted tumors in the mice was measured (e). Data represent the mean ± s.d. (two-way ANOVA). The tumors were weighed (f). Data represent the mean ± s.d. (one-way ANOVA). (g) IHC analyses of the indicated xenograft tumors from nude mice (n = 6) were performed with the indicated antibodies. Representative staining images are shown. a,b, Huh7 cells treated with indicated peptide (20 μM) were stimulated with or without LD. Immunoprecipitation and immunoblotting analyses with the indicated antibodies were performed; representative results from three independent experiments are shown. c-f, Huh7 cells (1 × 106) were subcutaneously administered into 6-week-old male athymic BALB/c nude mice (n = 6 per group). The resulting tumors were resected 28 days after injection (c). The growth of xenografted tumors in the mice was measured (d). Data represent the mean ± s.d. (two-way ANOVA). The tumors were weighed (e). Data represent the mean ± s.d. (one-way ANOVA). (f) IHC analyses of the indicated xenograft tumors from nude mice (n = 6) were performed with the indicated antibodies. Representative staining images are shown. g, IHC analyses of the indicated tumor samples were performed with an anti-Ki67 antibody (left). Ki67-positive cells were quantified (right) and quantification was averaged from the mean of each experiment. Bar graphs represent the percentage of Ki67-positive cells compared with MOCK group. Data represent the mean ± s.d. (n = 6) (one-way ANOVA). h, TUNEL analyses of the indicated tumor samples were performed. Apoptotic cells were stained brown (left) and quantified (right) and quantification was averaged from the mean of each experiment. Bar graphs represent the percentage of TUNEL-positive cells compared with MOCK group. Data represent the mean ± s.d. (n = 6) (one-way ANOVA).

ADSL promotes autophagy and tumor growth through fumarate-mediated Beclin1 dimethylation

Masan Group

Royal FrieslandCampina

Unilever

Loan

Nova Consumer Group is a leading company in the agricultural sector and the consumer goods industry. The company provides comprehensive and optimal solutions for farmers, including veterinary medicine, vaccines, and animal feed, and also offers safe and quality food products, beverages, and nutritional products. Nova Consumer Group primarily sells to the agricultural sector and the consumer goods industry. It was founded in 1992 and is based in Ho Chi Minh City, Vietnam.

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Date	1/14/2022	10/8/2015
Round	Loan	Unattributed
Amount	$17.5M	$XXM
Investors	DEG	Subscribe to see more
Valuation	$XXM	$XXM
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First funding	1/14/2022	00/00/0000
Last Funding	1/14/2022	00/00/0000
Investor	DEG	IFC
Rounds	1 Loan	Subscribe to see more
Board Seats
Type	Asset/Investment Management	Debt & Specialty Finance
Location	Germany	DC

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