Steven Zheng

Prof. Steven Zheng

Rutgers Cancer Institute of New Jersey, Rutgers University, New Brunswick, NJ, USA

Research Focus & Metrics

Academic Career Length

13Years (2014-Present)

(Calculated once Scilit publication data is synced: current year − year of first publication + 1)

Representative Publications

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19 March 2014 in Nature Communications
Verified
Journal Article
Open access
PDF file
Chi Kwan TsangChi Kwan Tsang
Chi Kwan Tsang
YLYuan Liu
Yuan Liu
JTJanice Thomas
Janice Thomas
YZYanjie Zhang
Yanjie Zhang
Steven ZhengSteven Zheng
Steven Zheng
Superoxide dismutase 1 (Sod1) has been known for nearly half a century for catalysis of superoxide to hydrogen peroxide. Here we report a new Sod1 function in oxidative signalling: in response to elevated endogenous and exogenous reactive oxygen species (ROS), Sod1 rapidly relocates into the nucleus, which is important for maintaining genomic stability. Interestingly, H2O2 is sufficient to promote Sod1 nuclear localization, indicating that it is responding to general ROS rather than Sod1 substrate superoxide. ROS signalling is mediated by Mec1/ATM and its effector Dun1/Cds1 kinase, through Dun1 interaction with Sod1 and regulation of Sod1 by phosphorylation at S60, 99. In the nucleus, Sod1 binds to promoters and regulates the expression of oxidative resistance and repair genes. Altogether, our study unravels an unorthodox function of Sod1 as a transcription factor and elucidates the regulatory mechanism for its localization.

1 November 2014 in Cancer Cell
Verified
Journal Article
Closed access
JTJanice D. Thomas
Janice D. Thomas
YZYan-Jie Zhang
Yan-Jie Zhang
YWYue-Hua Wei
Yue-Hua Wei
JCJun-Hung Cho
Jun-Hung Cho
LMLaura E. Morris
Laura E. Morris
Steven ZhengSteven Zheng
Steven Zheng

1 January 2016 in Drug Discovery Today
Verified
Journal Article
Closed access
MCMeixia Che
Meixia Che
RWRen Wang
Ren Wang
XLXiaoxing LI
Xiaoxing LI
HWHui-Yun Wang
Hui-Yun Wang
Steven ZhengSteven Zheng
Steven Zheng

3 May 2024 in Cells
Verified
Journal Article
Open access
PDF file
TZTinghan Zhao
Tinghan Zhao
JFJialin Fan
Jialin Fan
AAAhmed Abu-Zaid
Ahmed Abu-Zaid
SBStephen K. Burley
Stephen K. Burley
Steven ZhengSteven Zheng
Steven Zheng
MTOR is a central regulator of cell growth and metabolism in response to mitogenic and nutrient signals. Notably, mTOR is not only found in the cytoplasm but also in the nucleus. This review highlights direct involvement of nuclear mTOR in regulating transcription factors, orchestrating epigenetic modifications, and facilitating chromatin remodeling. These effects intricately modulate gene expression programs associated with growth and metabolic processes. Furthermore, the review underscores the importance of nuclear mTOR in mediating the interplay between metabolism and epigenetic modifications. By integrating its functions in nutrient signaling and gene expression related to growth and metabolism, nuclear mTOR emerges as a central hub governing cellular homeostasis, malignant transformation, and cancer progression. Better understanding of nuclear mTOR signaling has the potential to lead to novel therapies against cancer and other growth-related diseases.

19 May 2022 in European Journal of Cell Biology
Verified
Journal Article
Open access
JFJialin Fan
Jialin Fan
ZYZiqiang Yuan
Ziqiang Yuan
SBStephen K. Burley
Stephen K. Burley
SLSteven K. Libutti
Steven K. Libutti
Steven ZhengSteven Zheng
Steven Zheng
Amino Acids are not only major nutrient sources, but also serve as chemical signals to control cellular growth. Rab1A recently emerged as a key component in amino acid sensing and signaling to activate the mTOR complex1 (mTORC1). In a recently published study [1], we generated tamoxifen-inducible, conditional whole-body Rab1A knockout in adult mice. These mice are viable but develop hyperglycemia and glucose intolerance. Interestingly, Rab1A ablation selectively reduces insulin expression and pancreatic beta-cell population. Mechanistically, branched chain amino acids (BCAA), through the Rab1A-mTORC1 complex, promote the stability and nuclear localization of Pdx1, a master transcription factor that controls growth, function and identity of pancreatic beta-cells. These findings reveal a role and underlying mechanism by which amino acids control body’s glucose level through a beta-cell specific function by the Rab1A-mTORC1-Pdx1 signaling axis, which has implications in both diabetes and cancer.

12 January 2026 in Cell Reports
Verified
Journal Article
Open access
JFJialin Fan
Jialin Fan
XZXin Zhang
Xin Zhang
JZJinling Zhang
Jinling Zhang
TZTinghan Zhao
Tinghan Zhao
SBStephen K. Burley
Stephen K. Burley
Steven ZhengSteven Zheng
Steven Zheng
PDX1 is a key transcription factor regulating insulin expression in response to glucose. Our previous work showed that PDX1 is also stimulated by amino acids (aa). Here, we demonstrate that PDX1 broadly mediates aa-regulated transcriptional programs in β cells, especially those controlling β cell proliferation and function. Mechanistically, mTORC1 phosphorylates PDX1 at serine 61 (S61), enhancing its protein stability and transcriptional activity. A certain monogenic diabetes mutation disrupts this phosphorylation and impairs PDX1 function. To investigate its physiological role, we generated mice carrying S61A and S61E mutations, mimicking unphosphorylated and phosphorylated states. S61 phosphorylation promoted insulin expression and β cell proliferation, leading to Western diet-induced hyperinsulinemia, obesity, and hepatic steatosis. These findings reveal the central role of aa-mTORC1-PDX1 signaling in coordinating β cell proliferation and function under both physiological and pathological conditions.