USF2

Last update 08 May 2025

Basic Info

Synonyms

bHLHb12, Class B basic helix-loop-helix protein 12, FIP

+ [6]

Introduction

Transcription factor that binds to a symmetrical DNA sequence (E-boxes) (5'-CACGTG-3') that is found in a variety of viral and cellular promoters.

100 Clinical Results associated with USF2

100 Translational Medicine associated with USF2

0 Patents (Medical) associated with USF2

537

Literatures (Medical) associated with USF2

31 Mar 2025·International Heart Journal

Upstream Stimulatory Factor 2 Protects Cardiomyocytes by Regulating Mitochondrial Homeostasis

Article

Author: Li, Kejuan ; Ding, Hong ; Li, Yongnan ; Zhu, Ziwei ; Zhang, Xiaowei ; Chen, Jianshu ; Wu, Wenbin ; Zhao, Kexin

Myocardial ischemia and hypoxia are the main causes of heart failure, and cardiomyocyte apoptosis induced by mitochondrial injury is the basis of adverse heart remodeling and heart failure. Upstream stimulatory factor 2 (USF2), a transcription factor involved in multiple cellular processes, was recently shown to play an active role in mitochondrial function and energy homeostasis. However, its involvement in cardiovascular disease has not been previously reported. In this study, we demonstrated that under hypoxic conditions, USF2 protein expression can be degraded via the ubiquitin-proteasome pathway in cardiomyocytes. The deletion of USF2 results in mitochondrial dysfunction and exacerbates mitochondrial damage, ultimately promoting apoptosis. Mechanistically, we demonstrated that USF2 deficiency induces apoptosis in cells by modulating the AMPK/mTOR signaling pathway. In conclusion, this study provides new insights into the protective role of USF2 in hypoxic cardiomyocyte injury and indicates that USF2 could be a potential therapeutic target for myocardial hypoxia.

01 Mar 2025·The Journal of Gene Medicine

USF2‐Mediated Transcription of BZW2 Contributes to CRC Malignant Progression by Affecting LAMP3

Article

Author: Liu, Shuang ; Chen, Nanzheng ; Li, Xintao ; Liu, Yizhi

ABSTRACTBackgroundColorectal cancer (CRC) is one of the most frequent causes of cancer death in China, and its occurrence, development, and prognosis are closely related to the living state of patients. Basic leucine zipper and W2 domains 2 (BZW2), also known as eIF5‐mimin protein 1 (5MP1), is a translational regulatory protein and highly expressed in CRC and promotes malignant progression of CRC, but the specific mechanism has not been clarified.MethodsThe databases were used to mine related genes. The expression levels of genes were detected by quantitative real‐time PCR (qRT‐PCR) and western blot. 3‐(4,5‐Dimethyl‐2‐thiazolyl)‐2,5‐diphenyl tetrazolium bromide (MTT) assay, 5‐ethynyl‐2′‐deoxyuridine (EdU) staining, flow cytometry, transwell assay, and sphere formation assay were employed to examine the effects of BZW2 on the phenotypes in CRC cells in vitro. The mechanism of BZW2 in CRC progression was determined by chromatin immunoprecipitation (CHIP) and dual luciferase reporter assay. In vivo, xenograft animal model was performed to verify the results.ResultsBZW2 was elevated in CRC tissues and cells and was associated with poor prognosis of patients. Functionally, BZW2 enhanced CRC cell proliferation, invasion, and sphere formation but restrained apoptosis. CHIP and dual luciferase reporter assay confirmed that upstream transcription factor 2 (USF2) regulated BZW2 transcription. Also, BZW2 could attenuate the effects of USF2 defection in CRC progression. Meanwhile, lysosomal associated membrane protein 3 (LAMP3) acted as the target of BZW2 and restored the action of BZW2 knockdown. Similarly, BZW2 was involved in tumorigenesis in vivo by the same mechanism in vitro.ConclusionThese findings revealed a molecular basis for BZW2's promotion of CRC malignant progression and highlighted the role of BZW2 in promoting cancer stemness.

25 Feb 2025·Journal of Virology

RNASEK interacting with PEDV structural proteins facilitates virus entry via clathrin-mediated endocytosis

Article

Author: Kong, Ning ; Yu, Hai ; Wang, Yahe ; Tong, Wu ; Zhang, Wen ; Liu, Yuchang ; Zheng, Hao ; Cao, Xinyu ; Xie, Shengsong ; Liu, Hailong ; Qin, Wenzhen ; Yang, Xinyu ; Wang, Jiarui ; Shan, Tongling ; Tong, Guangzhi ; Sun, He

ABSTRACTPorcine epidemic diarrhea virus (PEDV), as a type of Alphacoronavirus causing acute diarrhea and high death rate among sucking piglets, poses great financial damage to the swine industry. Nevertheless, the molecular mechanism whereby PEDV enters host cells is unclear, limiting the development of PED vaccines and anti-PEDV agents. The present study found that the host protein ribonuclease kappa (RNASEK) was regulated by USF2, a transcription factor, and facilitated the PEDV replication. RNASEK was identified as a novel binding partner of PEDV, which interacted with a spike (S), envelope (E), and membrane (M) proteins on PEDV virion surfaces to increase the uptake not for attachment of PEDV virions. PEDV enters cells through the endocytosis pathways. RNASEK knockdown or RNASEK knockout assay revealed that through clathrin-mediated endocytosis (CME), RNASEK promoted the internalization of PEDV virions. Clathrin and the adaptor protein EPS15 only interacted with PEDV E protein, demonstrating that the RNASEK could target more virions through interaction with PEDV S, E, and M proteins to clathrin and EPS15 proteins rather than merely interacting with PEDV E protein to mediate the PEDV entry through CME. Moreover, our findings suggest that RNASEK, a newly identified host-entry factor, facilitates PEDV internalization by increasing the interaction of PEDV virions and EPS15-clathrin complex and may also provide a potential target for anti-PEDV therapies.IMPORTANCEPEDV is the causative pathogen of porcine diarrhea, which is a highly infectious acute intestinal condition, that poses significant economic damage to the swine industry. However, the existing PED vaccines fail to provide adequate protection for piglets against PEDV infection. Although PEDV replication in cells has been widely described, the mechanisms beneath PEDV entry of the host cells are incompletely understood. In this study, we showed that RNASEK, regulated by the transcription factor USF2, is a new host factor increasing PEDV infection in LLC-PK1 cells. RNASEK can bind to multiple structural proteins of PEDV (S, E, and M proteins), therefore increasing the interaction between PEDV virions, clathrin, and EPS15 to promote PEDV virion entry. Apart from unraveling the entry mechanisms of PEDV, our findings also contributed to facilitating the development of anti-PEDV agents and PED vaccines.

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USF2

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