PRMT4 drives post-ischemic angiogenesis via YB1/VEGF signaling

Yan, Shu; Ji, Hu; Li, Jia; Wang, Pengchao; Wang, Yilong; Wang, Zhaohui

doi:10.1007/s00109-021-02067-1

Cited by 11 publications

(16 citation statements)

References 35 publications

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“…PRMT5 was reported to catalyze the methylation of YB-1 at R205, which is crucial for NF-κB activation and downstream target gene expression [ 170 ]. Interestingly, PRMT4 interacts with YB-1 to activate VEGF transcription to accelerate angiogenesis; however, no actual methylation of YB-1 was identified in the study [ 171 ].…”

Section: Upstream Regulation Of Yb-1mentioning

confidence: 99%

YB-1 as an Oncoprotein: Functions, Regulation, Post-Translational Modifications, and Targeted Therapy

Yin

Zheng

Luo

et al. 2022

Cells

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Y box binding protein 1 (YB-1) is a protein with a highly conserved cold shock domain (CSD) that also belongs to the family of DNA- and RNA-binding proteins. YB-1 is present in both the nucleus and cytoplasm and plays versatile roles in gene transcription, RNA splicing, DNA damage repair, cell cycle progression, and immunity. Cumulative evidence suggests that YB-1 promotes the progression of multiple tumor types and serves as a potential tumor biomarker and therapeutic target. This review comprehensively summarizes the emerging functions, mechanisms, and regulation of YB-1 in cancers, and further discusses targeted strategies.

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Section: Upstream Regulation Of Yb-1mentioning

confidence: 99%

YB-1 as an Oncoprotein: Functions, Regulation, Post-Translational Modifications, and Targeted Therapy

Yin

Zheng

Luo

et al. 2022

Cells

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“…Nine members have been identi ed in the PRMT family, and PRMT4 is the only one targeting substrates with proline-rich motifs [13,14]. Previous studies showed that PRMT4 was bound with multiple transcription factors to participate in various bioprocess [12]. However, recent publications uncovered the non-transcription-related functions of PRMT4, including autophagy, early development, and mRNA metabolism [13].…”

Section: Introductionmentioning

confidence: 99%

PRMT4 interacts with NCOA4 to inhibit ferritinophagy in cisplatin-induced acute kidney injury

Zhou

Wang²,

Zhang

et al. 2023

Preprint

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Cisplatin-induced acute kidney injury (AKI) is commonly seen in clinical practice. Ferroptosis, an iron-catalyzed non-apoptotic cell death, is operative in the occurrence of cisplatin-induced AKI. Protein arginine methyltransferase (PRMT4), a member of type I PRMT family, was incorporated in various bioprocesses, but its role in renal injuries has not been investigated. In the present study, we aimed to explore the role of PRMT4 in cisplatin-induced AKI and its mechanism involved. Our data showed that PRMT4 was highly expressed in renal proximal tubular cells, and it was downregulated in cisplatin-induced AKI. Besides, genetic disruption of PRMT4 exacerbated, while its overexpression attenuated, cisplatin-induced redox injuries in renal proximal epithelia. Mechanistically, our work showed that PRMT4 interacted with NCOA4 to inhibit ferritinophagy, a process favoring lipid peroxidation to accelerate ferroptosis. Taken together, our study demonstrated that PRMT4 was bound to NCOA4 to attenuate ferroptosis in cisplatin-induced AKI, suggesting that PRMT4 might present as a new therapeutic target for cisplatin-related nephropathy.

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“…Emerging evidence indicates that PRMTs play broad functional roles in the regulation of endothelial cell function and angiogenesis. For example, endothelial-specific loss of PRMT1 in mice resulted in angiodysplasia ( Ishimaru et al., 2017 ), and PRMT4 has been shown to positively regulate angiogenesis by upregulating VEGF expression ( Yan et al., 2021 ). Similarly, the expression of PRMT5 is required for vasculogenesis in zebrafish ( Quillien et al., 2021 ).…”

Section: Discussionmentioning

confidence: 99%

“…Methylation of Arg and Lys is catalyzed by protein arginine methyltransferases (PRMTs) and lysine methyltransferases (KMTs), respectively. Previous studies have shown that PRMTs play key roles in the regulation of angiogenesis; endothelial-specific loss of PRMT1 in mice causes angiodysplasia ( Ishimaru et al., 2017 ), PRMT4 activity is linked to upregulation of VEGF ( Yan et al., 2021 ), and inhibition of PRMTs via pharmacological agents blocks angiogenesis ( Balcerczyk et al., 2016 ).…”

Section: Introductionmentioning

confidence: 99%

PRMT4-mediated arginine methylation promotes tyrosine phosphorylation of VEGFR-2 and regulates filopodia protrusions

et al. 2022

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PRMT4 drives post-ischemic angiogenesis via YB1/VEGF signaling

Cited by 11 publications

References 35 publications

YB-1 as an Oncoprotein: Functions, Regulation, Post-Translational Modifications, and Targeted Therapy

YB-1 as an Oncoprotein: Functions, Regulation, Post-Translational Modifications, and Targeted Therapy

PRMT4 interacts with NCOA4 to inhibit ferritinophagy in cisplatin-induced acute kidney injury

PRMT4-mediated arginine methylation promotes tyrosine phosphorylation of VEGFR-2 and regulates filopodia protrusions

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