RNASEK

Last update 08 May 2025

Basic Info

Synonyms

MGC71993, ribonuclease K, Ribonuclease kappa

+ [5]

Introduction

Endoribonuclease which preferentially cleaves ApU and ApG phosphodiester bonds. Hydrolyzes UpU bonds at a lower rate (PubMed:17881363). Regulates the activity of vacuolar (H+)-ATPase (V-ATPase) which is responsible for acidifying and maintaining the pH of intracellular compartments (PubMed:26212330). Required at an early stage of receptor-mediated endocytosis (PubMed:26212330). (Microbial infection) Required at an early stage of both clathrin-mediated and clathrin-independent endocytic uptake of a diverse set of viruses, including dengue, West Nile, Sindbis, Rift Valley Fever, influenza, and human rhinoviruses (PubMed:26056282, PubMed:26212330).

100 Clinical Results associated with RNASEK

100 Translational Medicine associated with RNASEK

0 Patents (Medical) associated with RNASEK

Literatures (Medical) associated with RNASEK

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.

18 Jan 2022·Journal of Clinical Investigation

RSPO2 and RANKL signal through LGR4 to regulate osteoclastic premetastatic niche formation and bone metastasis

Article

Author: Gao, Yankun ; Hu, Guohong ; Siwko, Stefan ; Niu, Xin ; He, Liang ; Zhang, Xiang H-F ; Li, Zhenxi ; Luo, Jian ; Liu, Mingyao ; Wang, Ning ; Ding, Yi ; Yue, Fei ; Jiang, Wenhao ; Gartland, Alison ; Xu, Ziwei ; Liu, Yanxi ; Qin, Qin ; Wang, Yi ; Xue, Xiwen ; Xiao, Jianru ; Li, Yi ; Chen, Geng ; Yue, Zhiying ; Yuan, Zengjin ; Li, Rong ; Yang, Zhengfeng ; Gao, Jingduo

Therapeutics targeting osteoclasts are commonly used treatments for bone metastasis; however, whether and how osteoclasts regulate premetastatic niche and bone tropism are largely unknown. In this study, we report that osteoclast precursors (OPs) can function as a premetastatic niche component that facilitates breast cancer (BCa) bone metastasis at early stages. At the molecular level, unbiased GPCR ligand/agonist screening in BCa cells suggested that R-spondin 2 (RSPO2) and RANKL, through interaction with their receptor LGR4, promoted osteoclastic premetastatic niche formation and enhanced BCa bone metastasis. This was achieved by RSPO2/RANKL-LGR4 signal modulating the WNT inhibitor DKK1 through Gαq and β-catenin signaling. DKK1 directly facilitated OP recruitment through suppression of its receptor LDL receptor-related protein 5 (LRP5) but not LRP6, upregulating Rnasek expression via inhibition of canonical WNT signaling. In clinical samples, RSPO2, LGR4, and DKK1 expression showed a positive correlation with BCa bone metastasis. Furthermore, soluble LGR4 extracellular domain (ECD) protein, acting as a decoy receptor for RSPO2 and RANKL, significantly alleviated bone metastasis and osteolytic lesions in a mouse bone metastasis model. These findings provide unique insights into the functional role of OPs as key components of the premetastatic niche for BCa bone metastasis and identify RSPO2/RANKL-LGR4 signaling as a promising target for inhibiting BCa bone metastasis.

01 Jan 2020·GenomicsQ3 · BIOLOGY

Identification of novel alternative transcripts of the human Ribonuclease κ (RNASEK) gene using 3′ RACE and high-throughput sequencing approaches

Q3 · BIOLOGY

Article

Author: Kontos, Christos K ; Sideris, Diamantis C ; Adamopoulos, Panagiotis G ; Scorilas, Andreas

The human RNASEK gene encodes Ribonuclease κ, an endoribonuclease that belongs to a highly conserved protein family of metazoans. Recent evidence suggests that the mRNA levels of the RNASEK gene possess biomarker attributes in patients with prostate cancer. In the present study, we used 3' RACE and next-generation sequencing (NGS) to detect and identify novel RNASEK transcripts. Computational analysis of the NGS data revealed new alternative splicing events that support the existence of novel RNASEK alternative transcripts. As a result, eight RNASEK splice variants were discovered and their expression profile was analyzed with the use of nested PCR in a wide panel of human cell lines, originating from several cancerous and/or normal human tissues. Based on in silico analysis, six of the eight novel RNASEK transcripts are predicted to encode new protein isoforms, while the remaining two splice variants could be considered as nonsense-mediated mRNA decay (NMD) candidates.

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RNASEK

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