Unlocking the Potential of IGF2BP1 as a Drug Target and Biomarker

Target Name: IGF2BP1

NCBI ID: G10642

Unlocking the Potential of IGF2BP1 as a Drug Target and Biomarker

Introduction

The insulin-like growth factor 2 (IGF2) signaling pathway is a crucial regulator of cellular growth, development, and metabolism. The IGF2BP1 gene, located on chromosome 1p36.1, has been identified as a potential drug target and biomarker for various diseases, including cancer, neurodegenerative disorders, and obesity. In this article, we will explore the IGF2BP1 molecule, its functions, and the potential of IGF2BP1 as a drug target and biomarker.

The IGF2BP1 Molecule and Its Functions

IGF2BP1 is a 21-kDa protein that contains 214 amino acid residues. It is a member of the IGF2 family, which includes several structurally similar proteins, including IGF1, IGF2, and IGF3. These proteins are involved in the regulation of cellular growth, differentiation , and survival. IGF2BP1 is characterized by a unique N-terminal domain, which consists of a single amino acid residue (Ala-214) and a hydrophobic tail.

IGF2BP1 is involved in several cellular processes, including cell signaling, cell adhesion, and cell survival. It plays a critical role in the regulation of cellular proliferation, differentiation, and survival. IGF2BP1 has been shown to promote cell survival by increasing the expression of the anti-apoptotic protein Bcl-2. Additionally, IGF2BP1 has been shown to regulate cell proliferation by suppressing the anti-proliferative protein p21.

IGF2BP1 has also been shown to play a role in cell adhesion. It is a structural component of the adherens junction, which is a complex protein structure that links adjacent cells and plays a critical role in cell-cell adhesion. IGF2BP1 has been shown to interact with the adhesion protein cadherin and promote the formation of the adherens junction.

Drug Targeting and Biomarker Potential

The IGF2BP1 molecule has been identified as a potential drug target due to its unique structure and its involvement in several cellular processes. One of the main goals of drug targeting is to inhibit the function of a protein and reduce its expression or activity. This can lead to the inhibition of the disease process and potentially lead to a therapeutic benefit.

IGF2BP1 has been shown to be a potential drug target by several studies. First, several studies have shown that IGF2BP1 can be inhibited by small molecules, including inhibitors of the IGF2BP1-ASF signaling pathway. Second, IGF2BP1 has been shown to be a potential biomarker for several diseases, including cancer, neurodegenerative disorders, and obesity.

One of the most promising aspects of IGF2BP1 as a drug target is its potential to treat several diseases, including cancer. IGF2BP1 has been shown to promote the growth and survival of cancer cells, making it a potential target for cancer therapies. Several studies have shown that inhibitors of IGF2BP1 can be effective in inhibiting the growth and survival of cancer cells.

Another promising aspect of IGF2BP1 as a drug target is its potential to treat neurodegenerative disorders. IGF2BP1 has been shown to contribute to the development and progression of several neurodegenerative disorders, including Alzheimer's disease and Parkinson's disease.

IGF2BP1 has also been shown to be a potential biomarker for obesity. Several studies have shown that IGF2BP1 levels are increased in obese individuals compared to normal individuals. Additionally, IGF2BP1 has

Protein Name: Insulin Like Growth Factor 2 MRNA Binding Protein 1

Functions: RNA-binding factor that recruits target transcripts to cytoplasmic protein-RNA complexes (mRNPs). This transcript 'caging' into mRNPs allows mRNA transport and transient storage. It also modulates the rate and location at which target transcripts encounter the translational apparatus and shields them from endonuclease attacks or microRNA-mediated degradation. Preferentially binds to N6-methyladenosine (m6A)-containing mRNAs and increases their stability (PubMed:29476152, PubMed:32245947). Plays a direct role in the transport and translation of transcripts required for axonal regeneration in adult sensory neurons (By similarity). Regulates localized beta-actin/ACTB mRNA translation, a crucial process for cell polarity, cell migration and neurite outgrowth. Co-transcriptionally associates with the ACTB mRNA in the nucleus. This binding involves a conserved 54-nucleotide element in the ACTB mRNA 3'-UTR, known as the 'zipcode'. The RNP thus formed is exported to the cytoplasm, binds to a motor protein and is transported along the cytoskeleton to the cell periphery. During transport, prevents ACTB mRNA from being translated into protein. When the RNP complex reaches its destination near the plasma membrane, IGF2BP1 is phosphorylated. This releases the mRNA, allowing ribosomal 40S and 60S subunits to assemble and initiate ACTB protein synthesis. Monomeric ACTB then assembles into the subcortical actin cytoskeleton (By similarity). During neuronal development, key regulator of neurite outgrowth, growth cone guidance and neuronal cell migration, presumably through the spatiotemporal fine tuning of protein synthesis, such as that of ACTB (By similarity). May regulate mRNA transport to activated synapses (By similarity). Binds to and stabilizes ABCB1/MDR-1 mRNA (By similarity). During interstinal wound repair, interacts with and stabilizes PTGS2 transcript. PTGS2 mRNA stabilization may be crucial for colonic mucosal wound healing (By similarity). Binds to the 3'-UTR of IGF2 mRNA by a mechanism of cooperative and sequential dimerization and regulates IGF2 mRNA subcellular localization and translation. Binds to MYC mRNA, in the coding region instability determinant (CRD) of the open reading frame (ORF), hence preventing MYC cleavage by endonucleases and possibly microRNA targeting to MYC-CRD (PubMed:29476152). Binding to MYC mRNA is enhanced by m6A-modification of the CRD (PubMed:29476152). Binds to the 3'-UTR of CD44 mRNA and stabilizes it, hence promotes cell adhesion and invadopodia formation in cancer cells. Binds to the oncofetal H19 transcript and to the neuron-specific TAU mRNA and regulates their localizations. Binds to and stabilizes BTRC/FBW1A mRNA. Binds to the adenine-rich autoregulatory sequence (ARS) located in PABPC1 mRNA and represses its translation. PABPC1 mRNA-binding is stimulated by PABPC1 protein. Prevents BTRC/FBW1A mRNA degradation by disrupting microRNA-dependent interaction with AGO2. Promotes the directed movement of tumor-derived cells by fine-tuning intracellular signaling networks. Binds to MAPK4 3'-UTR and inhibits its translation. Interacts with PTEN transcript open reading frame (ORF) and prevents mRNA decay. This combined action on MAPK4 (down-regulation) and PTEN (up-regulation) antagonizes HSPB1 phosphorylation, consequently it prevents G-actin sequestration by phosphorylated HSPB1, allowing F-actin polymerization. Hence enhances the velocity of cell migration and stimulates directed cell migration by PTEN-modulated polarization. Interacts with Hepatitis C virus (HCV) 5'-UTR and 3'-UTR and specifically enhances translation at the HCV IRES, but not 5'-cap-dependent translation, possibly by recruiting eIF3. Interacts with HIV-1 GAG protein and blocks the formation of infectious HIV-1 particles. Reduces HIV-1 assembly by inhibiting viral RNA packaging, as well as assembly and processing of GAG protein on cellular membranes. During cellular stress, such as oxidative stress or heat shock, stabilizes target mRNAs that are recruited to stress granules, including CD44, IGF2, MAPK4, MYC, PTEN, RAPGEF2 and RPS6KA5 transcripts

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