YTHDF2: A N6-Methyladenosine RNA Binding Protein 2 with Potential as a Drug Target or Biomarker

Target Name: YTHDF2

NCBI ID: G51441

YTHDF2

YTHDF2: A N6-Methyladenosine RNA Binding Protein 2 with Potential as a Drug Target or Biomarker

Abstract:

YTHDF2, or YTH N6-methyladenosine RNA binding protein 2, is a protein that has been identified as a potential drug target or biomarker. Its unique structure and function make it an intriguing candidate for further research. In this article, we will explore the structure and function of YTHDF2, its potential implications as a drug target or biomarker, and current research efforts to target this protein.

Introduction:

YTHDF2 is a protein that was identified as a potential drug target or biomarker using RNA sequencing (RNA-seq) data. It is a nuclear protein that is expressed in various tissues and has been shown to play a role in various cellular processes, including cell growth, apoptosis, and inflammation.

Structure and Function:

YTHDF2 is a 21-kDa protein that consists of 155 amino acid residues. It has a unique structure, with a distinct N-terminal domain that is rich in conserved putative transmembrane/extracellular domain interactions. The N-terminal domain is responsible for the protein's ability to interact with various RNA molecules, including adenosine.

The YTHDF2 protein has been shown to interact with several different RNA species, including microRNA (miRNA), long non-coding RNA (lncRNA), and RNA viruses. These interactions are important for the regulation of various cellular processes, including cell growth, apoptosis, and inflammation.

Potential Drug Target or Biomarker:

The unique structure and function of YTHDF2 make it an intriguing candidate as a drug target or biomarker. Its N-terminal domain, which is rich in conserved putative transmembrane/extracellular domain interactions, suggests that it may have multiple interaction sites that could be targeted by small molecules. Additionally, its role in the regulation of cellular processes that are altered in various diseases, such as cancer and neurodegenerative diseases, makes it an attractive target for drug development.

Current Research Efforts:

Current research efforts are focused on the characterization of YTHDF2 as a drug target or biomarker. Researchers have used various techniques, including RNA-seq, to identify potential drug targets for YTHDF2, including the inhibition of its N-terminal domain using small molecules and the use of antibodies to block its interaction with specific RNA species.

Additionally, researchers have used techniques such as mass spectrometry and affinity purification to identify potential biomarkers for YTHDF2, including the quantification of its protein levels and its ability to bind to specific RNA species.

Conclusion:

In conclusion, YTHDF2 is a protein that has shown promise as a drug target or biomarker. Its unique structure and function make it an intriguing candidate for further research. Further studies are needed to fully understand its potential as a drug target or biomarker.

Protein Name: YTH N6-methyladenosine RNA Binding Protein 2

Functions: Specifically recognizes and binds N6-methyladenosine (m6A)-containing RNAs, and regulates their stability (PubMed:24284625, PubMed:26046440, PubMed:26318451, PubMed:32492408). M6A is a modification present at internal sites of mRNAs and some non-coding RNAs and plays a role in mRNA stability and processing (PubMed:22575960, PubMed:24284625, PubMed:32492408, PubMed:25412658, PubMed:25412661). Acts as a regulator of mRNA stability by promoting degradation of m6A-containing mRNAs via interaction with the CCR4-NOT and ribonuclease P/MRP complexes, depending on the context (PubMed:24284625, PubMed:26046440, PubMed:27558897, PubMed:30930054, PubMed:32492408). The YTHDF paralogs (YTHDF1, YTHDF2 and YTHDF3) share m6A-containing mRNAs targets and act redundantly to mediate mRNA degradation and cellular differentiation (PubMed:28106072, PubMed:32492408). M6A-containing mRNAs containing a binding site for RIDA/HRSP12 (5'-GGUUC-3') are preferentially degraded by endoribonucleolytic cleavage: cooperative binding of RIDA/HRSP12 and YTHDF2 to transcripts leads to recruitment of the ribonuclease P/MRP complex (PubMed:30930054). Other m6A-containing mRNAs undergo deadenylation via direct interaction between YTHDF2 and CNOT1, leading to recruitment of the CCR4-NOT and subsequent deadenylation of m6A-containing mRNAs (PubMed:27558897). Required maternally to regulate oocyte maturation: probably acts by binding to m6A-containing mRNAs, thereby regulating maternal transcript dosage during oocyte maturation, which is essential for the competence of oocytes to sustain early zygotic development (By similarity). Also required during spermatogenesis: regulates spermagonial adhesion by promoting degradation of m6A-containing transcripts coding for matrix metallopeptidases (By similarity). Also involved in hematopoietic stem cells specification by binding to m6A-containing mRNAs, leading to promote their degradation (PubMed:30065315). Also acts as a regulator of neural development by promoting m6A-dependent degradation of neural development-related mRNA targets (By similarity). Inhibits neural specification of induced pluripotent stem cells by binding to methylated neural-specific mRNAs and promoting their degradation, thereby restraining neural differentiation (PubMed:32169943). Regulates circadian regulation of hepatic lipid metabolism: acts by promoting m6A-dependent degradation of PPARA transcripts (PubMed:30428350). Regulates the innate immune response to infection by inhibiting the type I interferon response: acts by binding to m6A-containing IFNB transcripts and promoting their degradation (PubMed:30559377). May also act as a promoter of cap-independent mRNA translation following heat shock stress: upon stress, relocalizes to the nucleus and specifically binds mRNAs with some m6A methylation mark at their 5'-UTR, protecting demethylation of mRNAs by FTO, thereby promoting cap-independent mRNA translation (PubMed:26458103). Regulates mitotic entry by promoting the phase-specific m6A-dependent degradation of WEE1 transcripts (PubMed:32267835). Promotes formation of phase-separated membraneless compartments, such as P-bodies or stress granules, by undergoing liquid-liquid phase separation upon binding to mRNAs containing multiple m6A-modified residues: polymethylated mRNAs act as a multivalent scaffold for the binding of YTHDF proteins, juxtaposing their disordered regions and thereby leading to phase separation (PubMed:31388144, PubMed:31292544, PubMed:32451507, PubMed:31642031). The resulting mRNA-YTHDF complexes then partition into different endogenous phase-separated membraneless compartments, such as P-bodies, stress granules or neuronal RNA granules (PubMed:31292544). May also recognize and bind RNAs modified by C5-methylcytosine (m5C) and act as a regulator of rRNA processing (PubMed:31815440)

The "YTHDF2 Target / Biomarker Review Report" is a customizable review of hundreds up to thousends of related scientific research literature by AI technology, covering specific information about YTHDF2 comprehensively, including but not limited to:
•   general information;
•   protein structure and compound binding;
•   protein biological mechanisms;
•   its importance;
•   the target screening and validation;
•   expression level;
•   disease relevance;
•   drug resistance;
•   related combination drugs;
•   pharmacochemistry experiments;
•   related patent analysis;
•   advantages and risks of development, etc.
The report is helpful for project application, drug molecule design, research progress updates, publication of research papers, patent applications, etc. If you are interested to get a full version of this report, please feel free to contact us at BD@silexon.ai

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