FMR1: A Protein Involved in Cellular Signaling and Metabolism

Target Name: FMR1

NCBI ID: G2332

FMR1

FMR1: A Protein Involved in Cellular Signaling and Metabolism

FMR1 (FMR1_HUMAN) is a gene that encodes a protein known as fragile mitochondrial receptor 1. FMR1 is a protein that is expressed in the heart, brain, and other tissues of the body. It is a key regulator of mitochondrial function and has been implicated in a number of diseases, including Alzheimer's disease, Parkinson's disease, and cardiomyopathy.

FMR1 is also a potential drug target for several pharmaceutical companies. Its unique structure and function make it an attractive target for small molecules, antibodies, and other therapeutic agents. The protein is also a good candidate for imaging agents, which could be used to detect and diagnose diseases associated with FMR1 dysfunction.

FMR1 is a transmembrane protein that is expressed in the mitochondria. It consists of an extracellular domain, a transmembrane domain, and an intracellular domain. The extracellular domain is the part of the protein that is exposed to the outside of the cell, while the transmembrane domain is the part that spans the membrane of the mitochondria. The intracellular domain is the part of the protein that interacts with the mitochondrial cytosol.

FMR1 is involved in a number of important cellular processes. It is a regulator of mitochondrial fusion, which is the process by which new mitochondria are formed in the cell. It is also involved in the regulation of mitochondrial fission, which is the process by which one mitochondrion is divided into two.

FMR1 is also involved in the regulation of mitochondrial dynamics. It helps to control the movement of mitochondria into the cytoplasm and out of the mitochondria, which is important for maintaining cellular homeostasis.

FMR1 is also involved in the regulation of cellular signaling pathways. It is a negative regulator of the protein kinase B, which is a key regulator of cell growth and survival. It is also a positive regulator of the protein p21, which is involved in the regulation of cell cycle progression.

FMR1 is also involved in the regulation of cellular metabolism. It is a regulator of the metabolism of fatty acids, which are an important source of energy for the cell. It is also involved in the regulation of carbohydrate metabolism, which is the process by which the cell converts carbohydrates into energy.

FMR1 is also involved in the regulation of cellular immune response. It is a regulator of the production of pro-inflammatory cytokines, which are important for the immune response. It is also involved in the regulation of the production of anti-inflammatory cytokines, which help to counteract the pro-inflammatory effects of cytokines.

FMR1 is a unique protein that plays an important role in cellular function. Its structure and function make it an attractive target for small molecules, antibodies, and other therapeutic agents. The potential drug targets for FMR1 are vast, and its unique properties make it an exciting area of 鈥嬧?媟esearch.

Protein Name: Fragile X Messenger Ribonucleoprotein 1

Functions: Multifunctional polyribosome-associated RNA-binding protein that plays a central role in neuronal development and synaptic plasticity through the regulation of alternative mRNA splicing, mRNA stability, mRNA dendritic transport and postsynaptic local protein synthesis of target mRNAs (PubMed:12417522, PubMed:16631377, PubMed:18653529, PubMed:19166269, PubMed:23235829, PubMed:25464849). Acts as an mRNA regulator by mediating formation of some phase-separated membraneless compartment: undergoes liquid-liquid phase separation upon binding to target mRNAs, leading to assemble mRNAs into cytoplasmic ribonucleoprotein granules that concentrate mRNAs with associated regulatory factors (PubMed:12417522, PubMed:30765518, PubMed:31439799). Plays a role in the alternative splicing of its own mRNA (PubMed:18653529). Stabilizes the scaffolding postsynaptic density protein DLG4/PSD-95 and the myelin basic protein (MBP) mRNAs in hippocampal neurons and glial cells, respectively; this stabilization is further increased in response to metabotropic glutamate receptor (mGluR) stimulation (By similarity). Plays a role in selective delivery of a subset of dendritic mRNAs to synaptic sites in response to mGluR activation in a kinesin-dependent manner (By similarity). Undergoes liquid-liquid phase separation following phosphorylation and interaction with CAPRIN1, promoting formation of cytoplasmic ribonucleoprotein granules that concentrate mRNAs with factors that inhibit translation and mediate deadenylation of target mRNAs (PubMed:31439799). Acts as a repressor of mRNA translation in synaptic regions by mediating formation of neuronal ribonucleoprotein granules and promoting recruitmtent of EIF4EBP2 (PubMed:30765518). Plays a role as a repressor of mRNA translation during the transport of dendritic mRNAs to postsynaptic dendritic spines (PubMed:11532944, PubMed:11157796, PubMed:12594214, PubMed:23235829). Component of the CYFIP1-EIF4E-FMR1 complex which blocks cap-dependent mRNA translation initiation (By similarity). Represses mRNA translation by stalling ribosomal translocation during elongation (By similarity). Reports are contradictory with regards to its ability to mediate translation inhibition of MBP mRNA in oligodendrocytes (PubMed:23891804). Also involved in the recruitment of the RNA helicase MOV10 to a subset of mRNAs and hence regulates microRNA (miRNA)-mediated translational repression by AGO2 (PubMed:14703574, PubMed:17057366, PubMed:25464849). Facilitates the assembly of miRNAs on specific target mRNAs (PubMed:17057366). Also plays a role as an activator of mRNA translation of a subset of dendritic mRNAs at synapses (PubMed:19097999, PubMed:19166269). In response to mGluR stimulation, FMR1-target mRNAs are rapidly derepressed, allowing for local translation at synapses (By similarity). Binds to a large subset of dendritic mRNAs that encode a myriad of proteins involved in pre- and postsynaptic functions (PubMed:7692601, PubMed:11719189, PubMed:11157796, PubMed:12594214, PubMed:17417632, PubMed:23235829, PubMed:24448548). Binds to 5'-ACU[GU]-3' and/or 5'-[AU]GGA-3' RNA consensus sequences within mRNA targets, mainly at coding sequence (CDS) and 3'-untranslated region (UTR) and less frequently at 5'-UTR (PubMed:23235829). Binds to intramolecular G-quadruplex structures in the 5'- or 3'-UTRs of mRNA targets (PubMed:11719189, PubMed:18579868, PubMed:25464849, PubMed:25692235). Binds to G-quadruplex structures in the 3'-UTR of its own mRNA (PubMed:7692601, PubMed:11532944, PubMed:12594214, PubMed:15282548, PubMed:18653529). Binds also to RNA ligands harboring a kissing complex (kc) structure; this binding may mediate the association of FMR1 with polyribosomes (PubMed:15805463). Binds mRNAs containing U-rich target sequences (PubMed:12927206). Binds to a triple stem-loop RNA structure, called Sod1 stem loop interacting with FMRP (SoSLIP), in the 5'-UTR region of superoxide dismutase SOD1 mRNA (PubMed:19166269). Binds to the dendritic, small non-coding brain cytoplasmic RNA 1 (BC1); which may increase the association of the CYFIP1-EIF4E-FMR1 complex to FMR1 target mRNAs at synapses (By similarity). Plays a role in mRNA nuclear export (PubMed:31753916). Specifically recognizes and binds a subset of N6-methyladenosine (m6A)-containing mRNAs, promoting their nuclear export in a XPO1/CRM1-dependent manner (PubMed:31753916). Together with export factor NXF2, is involved in the regulation of the NXF1 mRNA stability in neurons (By similarity). Associates with export factor NXF1 mRNA-containing ribonucleoprotein particles (mRNPs) in a NXF2-dependent manner (By similarity). Binds to a subset of miRNAs in the brain (PubMed:14703574, PubMed:17057366). May associate with nascent transcripts in a nuclear protein NXF1-dependent manner (PubMed:18936162). In vitro, binds to RNA homomer; preferentially on poly(G) and to a lesser extent on poly(U), but not on poly(A) or poly(C) (PubMed:7688265, PubMed:7781595, PubMed:12950170, PubMed:153

The "FMR1 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 FMR1 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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