Target Name: YTHDF1
NCBI ID: G54915
Other Name(s): OTTHUMP00000031533 | dermatomyositis associated with cancer putative autoantigen 1 | YTH domain family, member 1 | YTH N(6)-methyladenosine RNA binding protein 1 | YTH domain family protein 1 | OTTHUMP00000031534 | YTH domain family 1 | YTH domain-containing family protein 1 | C20orf21 | FLJ20391 | YTH N6-methyladenosine RNA binding protein 1 | YTHD1_HUMAN | DF1 | DACA-1 | Dermatomyositis associated with cancer putative autoantigen 1

YTHDF1: The Potential Drug Target and Biomarker

Yet to be discovered and validated, YTHDF1 (short for Yet Another Transmembrane Protein F1) has the potential to be a drug target and biomarker. Its unique structure and various functions make it an interesting candidate for drug development. This article will discuss the YTHDF1 protein, its functions, potential drug targets, and its potential as a biomarker.

Structure and Functions

YTHDF1 is a protein that spans the membrane of various cell types, including neurons, endothelial cells, and epithelial cells. Its structure is quite unique, as it consists of a transmembrane domain and a cytoplasmic tail. The transmembrane domain is responsible for the protein's unique structure and its ability to interact with various intracellular signaling pathways.

YTHDF1 functions as a critical signaling molecule in various cell types. Its role in cell signaling cascades is crucial for the regulation of various cellular processes, including cell adhesion, migration, and angiogenesis. YTHDF1 has been shown to play a vital role in the regulation of neuronal communication, which is critical for the development and progression of various neurological diseases.

Potential Drug Targets

YTHDF1's unique structure and various functions make it an attractive drug target. Its transmembrane domain and cytoplasmic tail make it a potential receptor for small molecules, making it a strong candidate for drug development. Additionally, its functions in cell signaling cascades make it a potential target for molecules that regulate cell signaling pathways.

One of the promising candidates for YTHDF1 drug development is the small molecule drug, U-8712, which targets the Src/FAK signaling pathway. This pathway is involved in the regulation of cell adhesion, migration, and angiogenesis, making it a potential target for YTHDF1. U-8712 has been shown to increase the migration of cancer cells, which suggests that it may have potential as a cancer therapeutic.

Another potential drug target for YTHDF1 is the protein, FAK, which is involved in the regulation of cell adhesion, migration, and angiogenesis. FAK has been shown to interact with YTHDF1 and may play a role in the regulation of its functions. Therefore, targeting FAK with small molecules may be an effective way to inhibit the functions of YTHDF1.

Potential Biomarkers

YTHDF1 has the potential to serve as a biomarker for various diseases, including cancer. Its unique structure and various functions make it an attractive candidate for diagnostic biomarkers.

One of the potential biomarkers for YTHDF1 is its expression level. The expression level of YTHDF1 can be easily measured using various techniques, such as qRT-PCR, western blotting, and immunofluorescence. By analyzing the expression level of YTHDF1, researchers can monitor the effectiveness of various therapeutic approaches and monitor the response of cancer cells to different treatments.

Another potential biomarker for YTHDF1 is its function. By measuring the functions of YTHDF1, researchers can determine its role in various cellular processes and identify potential drug targets. For example, researchers can measure the migration and adhesion of cancer cells to determine the effectiveness of different therapeutic approaches.

Conclusion

YTHDF1 is a unique protein that has the potential to be a drug target and biomarker. Its unique structure and various functions make it an attractive candidate for drug development. The transmembrane domain and cytoplasmic tail make it a potential receptor for small molecules, while its role in cell signaling cascades and its potential as a biomarker make it an interesting candidate for drug development. Further research is needed to determine its role in various cellular processes and identify potential drug targets.

Protein Name: YTH N6-methyladenosine RNA Binding Protein 1

Functions: Specifically recognizes and binds N6-methyladenosine (m6A)-containing mRNAs, and regulates their stability (PubMed:24284625, PubMed:32492408, PubMed:26318451). 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:24284625, PubMed:32492408). Acts as a regulator of mRNA stability by promoting degradation of m6A-containing mRNAs via interaction with the CCR4-NOT complex (PubMed:32492408). The YTHDF paralogs (YTHDF1, YTHDF2 and YTHDF3) shares m6A-containing mRNAs targets and act redundantly to mediate mRNA degradation and cellular differentiation (PubMed:28106072, PubMed:32492408). Required to facilitate learning and memory formation in the hippocampus by binding to m6A-containing neuronal mRNAs (By similarity). Acts as a regulator of axon guidance by binding to m6A-containing ROBO3 transcripts (By similarity). Acts as a negative regulator of antigen cross-presentation in myeloid dendritic cells (By similarity). In the context of tumorigenesis, negative regulation of antigen cross-presentation limits the anti-tumor response by reducing efficiency of tumor-antigen cross-presentation (By similarity). 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). 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)

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YTHDF2 | YTHDF3 | YWHAB | YWHABP1 | YWHAE | YWHAEP1 | YWHAEP7 | YWHAG | YWHAH | YWHAH-AS1 | YWHAQ | YWHAQP6 | YWHAZ | YWHAZP2 | YWHAZP5 | YY1 | YY1AP1 | YY1P2 | YY2 | ZACN | ZAN | ZAP70 | ZAR1 | ZAR1L | ZBBX | ZBED1 | ZBED10P | ZBED2 | ZBED3 | ZBED3-AS1 | ZBED4 | ZBED5 | ZBED5-AS1 | ZBED6 | ZBP1 | ZBTB1 | ZBTB10 | ZBTB11 | ZBTB11-AS1 | ZBTB12 | ZBTB12BP | ZBTB14 | ZBTB16 | ZBTB17 | ZBTB18 | ZBTB2 | ZBTB20 | ZBTB21 | ZBTB22 | ZBTB24 | ZBTB25 | ZBTB26 | ZBTB3 | ZBTB32 | ZBTB33 | ZBTB34 | ZBTB37 | ZBTB38 | ZBTB39 | ZBTB4 | ZBTB40 | ZBTB41 | ZBTB42 | ZBTB43 | ZBTB44 | ZBTB44-DT | ZBTB45 | ZBTB45P2 | ZBTB46 | ZBTB46-AS1 | ZBTB47 | ZBTB48 | ZBTB49 | ZBTB5 | ZBTB6 | ZBTB7A | ZBTB7B | ZBTB7C | ZBTB7C-AS2 | ZBTB8A | ZBTB8B | ZBTB8OS | ZBTB8OSP1 | ZBTB9 | ZC2HC1A | ZC2HC1B | ZC2HC1C | ZC3H10 | ZC3H11A | ZC3H11B | ZC3H11C | ZC3H12A | ZC3H12A-DT | ZC3H12B | ZC3H12C | ZC3H12D | ZC3H13 | ZC3H14 | ZC3H15 | ZC3H18