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26 results on '"Luo, Yongbo"'

13. Fatty acid oxidation mediated by malonyl-CoA decarboxylase represses renal cell carcinoma progression

Author

Zhou, Lijie, primary, Luo, Yongbo, additional, Liu, Yuenan, additional, Zeng, Youmiao, additional, Tong, Junwei, additional, Li, Mengting, additional, Hou, Yaxin, additional, Du, Kaixuan, additional, Qi, Yabin, additional, Pan, Wenbang, additional, Liu, Yuanhao, additional, Wang, Rongli, additional, Tian, Fengyan, additional, Gu, Chaohui, additional, and Chen, Ke, additional

Published
2023
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16. Complex structure and activation mechanism of arginine kinase McsB by McsA

Author

Lu, Kai, Luo, Bingnan, Tao, Xuan, Luo, Yongbo, Ao, Mingjun, Zheng, Bin, Xu, Xiang, Ma, Xiaoyan, Niu, Jingling, Li, Huinan, Xie, Yanxuan, Zhao, Zhennan, Zheng, Peng, Wang, Guanbo, Gao, Song, Wang, Chao, Xia, Wei, Su, Zhaoming, and Mao, Zong-Wan

Abstract

Protein phosphorylation is a pivotal post-translational modification modulating various cellular processes. In Gram-positive bacteria, the protein arginine kinase McsB, along with its activator McsA, has a key role in labeling misfolded and damaged proteins during stress. However, the activation mechanism of McsB by McsA remains elusive. Here we report the cryo-electron microscopy structure of a tetrameric McsA–McsB complex at 3.41 Å resolution. Biochemical analysis indicates that the homotetrameric assembly is essential for McsB’s kinase activity. The conserved C-terminal zinc finger of McsA interacts with an extended loop in McsB, optimally orienting a critical catalytic cysteine residue. In addition, McsA binding decreases the CtsR’s affinity for McsB, enhancing McsB’s kinase activity and accelerating the turnover rate of CtsR phosphorylation. Furthermore, McsA binding also increases McsB’s thermostability, ensuring its activity under heat stress. These findings elucidate the structural basis and activation mechanism of McsB in stress response.

Published
2024
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17. Pseudomonas aeruginosaregulator PvrA binds simultaneously to multiple pseudo-palindromic sites for efficient transcription activation

Author

Zhu, Yibo, Luo, Bingnan, Mou, Xingyu, Song, Yingjie, Zhou, Yonghong, Luo, Yongbo, Sun, Bo, Luo, Youfu, Tang, Hong, Su, Zhaoming, and Bao, Rui

Abstract

Tetracycline repressor (TetR) family regulators (TFRs) are the largest group of DNA-binding transcription factors and are widely distributed in bacteria and archaea. TFRs play vital roles in controlling the expression of various genes and regulating diverse physiological processes. Recently, a TFR protein Pseudomonas virulence regulator A (PvrA), was identified from Pseudomonas aeruginosaas the transcriptional activator of genes involved in fatty acid utilization and bacterial virulence. Here, we show that PvrA can simultaneously bind to multiple pseudo-palindromic sites and upregulate the expression levels of target genes. Cryo-electron microscopy (cryo-EM) analysis indicates the simultaneous DNA recognition mechanism of PvrA and suggests that the bound DNA fragments consist of a distorted B-DNA double helix. The crystal structure and functional analysis of PvrA reveal a hinge region that secures the correct domain motion for recognition of the promiscuous promoter. Additionally, our results showed that mutations disrupting the regulatory hinge region have differential effects on biofilm formation and pyocyanin biosynthesis, resulting in attenuated bacterial virulence. Collectively, these findings will improve the understanding of the relationship between the structure and function of the TetR family and provide new insights into the mechanism of regulation of P. aeruginosavirulence.

Published
2024
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18. Structural basis of sRNA RsmZ regulation ofPseudomonas aeruginosavirulence

Author

Jia, Xinyu, primary, Pan, Zhiling, additional, Yuan, Yang, additional, Luo, Bingnan, additional, Luo, Yongbo, additional, Mukherjee, Sunandan, additional, Jia, Guowen, additional, Liu, Liu, additional, Ling, Xiaobin, additional, Yang, Xiting, additional, Miao, Zhichao, additional, Wei, Xiawei, additional, Bujnicki, Janusz M., additional, Zhao, Kelei, additional, and Su, Zhaoming, additional

Published
2022
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26. m6A-Mediated Induction of 7-Dehydrocholesterol Reductase Stimulates Cholesterol Synthesis and cAMP Signaling to Promote Bladder Cancer Metastasis.

Author

Zeng Y, Luo Y, Zhao K, Liu S, Wu K, Wu Y, Du K, Pan W, Dai Y, Liu Y, Ren M, Tian F, Zhou L, and Gu C

Subjects
Humans, Animals, Mice, Cell Line, Tumor, Mice, Nude, Neoplasm Metastasis, Cyclic AMP-Dependent Protein Kinases metabolism, Female, Gene Expression Regulation, Neoplastic, Male, Xenograft Model Antitumor Assays, Focal Adhesion Kinase 1 metabolism, Focal Adhesion Kinase 1 genetics, Mice, Inbred BALB C, Adenosine analogs & derivatives, Urinary Bladder Neoplasms pathology, Urinary Bladder Neoplasms metabolism, Urinary Bladder Neoplasms genetics, Cyclic AMP metabolism, Oxidoreductases Acting on CH-CH Group Donors metabolism, Oxidoreductases Acting on CH-CH Group Donors genetics, Cholesterol metabolism, Cholesterol biosynthesis, Signal Transduction
Abstract

Dysregulation of cholesterol homeostasis occurs in multiple types of tumors and promotes cancer progression. Investigating the specific processes that induce abnormal cholesterol metabolism could identify therapeutic targets to improve cancer treatment. In this investigation, we observed upregulation of 7-dehydrocholesterol reductase (DHCR7), a vital enzyme involved in the synthesis of cholesterol, within bladder cancer tissues in comparison to normal tissues, which was correlated with increased bladder cancer metastasis. Increased expression of DHCR7 in bladder cancer was attributed to decreased mRNA degradation mediated by YTHDF2. Loss or inhibition of DHCR7 reduced bladder cancer cell invasion in vitro and metastasis in vivo. Mechanistically, DHCR7 promoted bladder cancer metastasis by activating the cAMP/protein kinase A/FAK pathway. Specifically, DHCR7 increased cAMP levels by elevating cholesterol content in lipid rafts, thereby facilitating the transduction of signaling pathways mediated by cAMP receptors. DHCR7 additionally enhanced the cAMP signaling pathway by reducing the concentration of 7-dehydrocholesterol and promoting the transcription of the G protein-coupled receptor, namely gastric inhibitory polypeptide receptor. Overall, these findings demonstrate that DHCR7 plays an important role in bladder cancer invasion and metastasis by modulating cholesterol synthesis and cAMP signaling. Furthermore, inhibition of DHCR7 shows promise as a viable therapeutic strategy for suppressing bladder cancer invasion and metastasis. Significance: Inhibiting DHCR7 induces cholesterol metabolism reprogramming and lipid raft remodeling to inactivate the cAMP/protein kinase A/FAK axis and suppress bladder cancer metastasis, indicating the therapeutic potential of targeting DHCR7., (©2024 American Association for Cancer Research.)

Published
2024
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