MIR4436B2 Gene

Name microRNA 4436b-2
Description microRNAs (miRNAs) are short (20-24 nt) non-coding RNAs that are involved in post-transcriptional regulation of gene expression in multicellular organisms by affecting both the stability and translation of mRNAs. miRNAs are transcribed by RNA polymerase II as part of capped and polyadenylated primary transcripts (pri-miRNAs) that can be either protein-coding or non-coding. The primary transcript is cleaved by the Drosha ribonuclease III enzyme to produce an approximately 70-nt stem-loop precursor miRNA (pre-miRNA), which is further cleaved by the cytoplasmic Dicer ribonuclease to generate the mature miRNA and antisense miRNA star (miRNA*) products. The mature miRNA is incorporated into a RNA-induced silencing complex (RISC), which recognizes target mRNAs through imperfect base pairing with the miRNA and most commonly results in translational inhibition or destabilization of the target mRNA. The RefSeq represents the predicted microRNA stem-loop. [provided by RefSeq, Sep 2009]
Summary
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Early investigations established the critical importance of tropomyosin in both stabilizing filamentous actin and serving as an allosteric regulator of myosin binding in muscle thin filaments, laying the groundwork for understanding how changes in tropomyosin expression or structure may influence muscle performance and disease."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "1", "end_ref": "8"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nSubsequent studies have detailed how alterations in tropomyosin—whether through alternative splicing, point mutations, or post‐translational modifications like phosphorylation—directly impact contractile activity and sarcomeric integrity. For example, aberrant splicing mediated by factors such as PTB and raver1 alters tropomyosin isoform expression in a tissue–specific manner, while mutations that modify the charge or flexibility of tropomyosin (or its interactions with proteins such as troponin and myosin binding protein C) have been shown to elicit profound effects in disease models of hypertrophic cardiomyopathy and dilated cardiomyopathy. These observations underline a complex regulatory network in which fine‐tuning of tropomyosin function is essential for normal muscle physiology."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "9", "end_ref": "16"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nMoreover, broader physiological investigations have expanded the significance of tropomyosin regulation to include roles in cytoskeletal remodeling during aging, cellular differentiation in developmental and epithelial–mesenchymal transition contexts, and even hematopoiesis. These complex regulatory mechanisms provide a rationale for considering that MIR4436B2, as a putative microRNA regulator, could influence muscle performance and related cellular processes by targeting the transcripts or modulators of tropomyosin. Such microRNA–mediated modulation may adjust splicing patterns, stabilize select isoforms, or affect the post–translational modification profile of tropomyosin, thereby impacting the balance between contractility and relaxation as well as responses to physiological or pathological stress."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "17", "end_ref": "24"}]}, {"type": "t", "text": "\n"}]}, {"type": "rg", "children": [{"type": "r", "ref": 1, "children": [{"type": "t", "text": "Julian von der Ecken, Mirco Müller, William Lehman, et al. 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"}, {"type": "b", "children": [{"type": "t", "text": "Altered signaling surrounding the C-lobe of cardiac troponin C in myofilaments containing an alpha-tropomyosin mutation linked to familial hypertrophic cardiomyopathy."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "J Mol Cell Cardiol (2003)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1016/s0022-2828(03)00240-2"}], "href": "https://doi.org/10.1016/s0022-2828(03"}, {"type": "t", "text": "00240-2) PMID: "}, {"type": "a", "children": [{"type": "t", "text": "14519438"}], "href": "https://pubmed.ncbi.nlm.nih.gov/14519438"}]}, {"type": "r", "ref": 14, "children": [{"type": "t", "text": "Emily M Schulz, Richard N Correll, Hajer N Sheikh, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Tropomyosin dephosphorylation results in compensated cardiac hypertrophy."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "J Biol Chem (2012)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1074/jbc.M112.402040"}], "href": "https://doi.org/10.1074/jbc.M112.402040"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "23148217"}], "href": "https://pubmed.ncbi.nlm.nih.gov/23148217"}]}, {"type": "r", "ref": 15, "children": [{"type": "t", "text": "Ji Young Mun, Robert W Kensler, Samantha P Harris, et al. "}, {"type": "b", "children": [{"type": "t", "text": "The cMyBP-C HCM variant L348P enhances thin filament activation through an increased shift in tropomyosin position."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "J Mol Cell Cardiol (2016)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1016/j.yjmcc.2015.12.014"}], "href": "https://doi.org/10.1016/j.yjmcc.2015.12.014"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "26718724"}], "href": "https://pubmed.ncbi.nlm.nih.gov/26718724"}]}, {"type": "r", "ref": 16, "children": [{"type": "t", "text": "Rong Li, Yuxiang Liang, Bin Lin "}, {"type": "b", "children": [{"type": "t", "text": "Accumulation of systematic TPM1 mediates inflammation and neuronal remodeling by phosphorylating PKA and regulating the FABP5/NF-κB signaling pathway in the retina of aged mice."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Aging Cell (2022)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1111/acel.13566"}], "href": "https://doi.org/10.1111/acel.13566"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "35148456"}], "href": "https://pubmed.ncbi.nlm.nih.gov/35148456"}]}, {"type": "r", "ref": 17, "children": [{"type": "t", "text": "Shantaram Bharadwaj, Sarah Hitchcock-DeGregori, Andrew Thorburn, et al. "}, {"type": "b", "children": [{"type": "t", "text": "N terminus is essential for tropomyosin functions: N-terminal modification disrupts stress fiber organization and abolishes anti-oncogenic effects of tropomyosin-1."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "J Biol Chem (2004)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1074/jbc.M310934200"}], "href": "https://doi.org/10.1074/jbc.M310934200"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "14722123"}], "href": "https://pubmed.ncbi.nlm.nih.gov/14722123"}]}, {"type": "r", "ref": 18, "children": [{"type": "t", "text": "Rong Li, Jing Zhang, Qiong Wang, et al. "}, {"type": "b", "children": [{"type": "t", "text": "TPM1 mediates inflammation downstream of TREM2 via the PKA/CREB signaling pathway."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "J Neuroinflammation (2022)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1186/s12974-022-02619-3"}], "href": "https://doi.org/10.1186/s12974-022-02619-3"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "36241997"}], "href": "https://pubmed.ncbi.nlm.nih.gov/36241997"}]}, {"type": "r", "ref": 19, "children": [{"type": "t", "text": "Sudarsan Rajan, Ganapathy Jagatheesan, Natalia Petrashevskaya, et al. 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"}, {"type": "b", "children": [{"type": "t", "text": "Charged residue alterations in the inner-core domain and carboxy-terminus of alpha-tropomyosin differentially affect mouse cardiac muscle contractility."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "J Physiol (2004)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1113/jphysiol.2004.070631"}], "href": "https://doi.org/10.1113/jphysiol.2004.070631"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "15486021"}], "href": "https://pubmed.ncbi.nlm.nih.gov/15486021"}]}, {"type": "r", "ref": 21, "children": [{"type": "t", "text": "Felipe Hornos, Han-Zhong Feng, Bruno Rizzuti, et al. "}, {"type": "b", "children": [{"type": "t", "text": "The muscle-relaxing C-terminal peptide from troponin I populates a nascent helix, facilitating binding to tropomyosin with a potent therapeutic effect."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "J Biol Chem (2021)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1074/jbc.RA120.016012"}], "href": "https://doi.org/10.1074/jbc.RA120.016012"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "33814345"}], "href": "https://pubmed.ncbi.nlm.nih.gov/33814345"}]}, {"type": "r", "ref": 22, "children": [{"type": "t", "text": "Polakit Teekakirikul, Wenjuan Zhu, Xinxiu Xu, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Genetic resiliency associated with dominant lethal TPM1 mutation causing atrial septal defect with high heritability."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Cell Rep Med (2022)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1016/j.xcrm.2021.100501"}], "href": "https://doi.org/10.1016/j.xcrm.2021.100501"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "35243414"}], "href": "https://pubmed.ncbi.nlm.nih.gov/35243414"}]}, {"type": "r", "ref": 23, "children": [{"type": "t", "text": "Zhen-Xing Wang, Xiao Lin, Jia Cao, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Young osteocyte-derived extracellular vesicles facilitate osteogenesis by transferring tropomyosin-1."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "J Nanobiotechnology (2024)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1186/s12951-024-02367-x"}], "href": "https://doi.org/10.1186/s12951-024-02367-x"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "38664789"}], "href": "https://pubmed.ncbi.nlm.nih.gov/38664789"}]}, {"type": "r", "ref": 24, "children": [{"type": "t", "text": "Madison B Wilken, Gennadiy Fonar, Rong Qiu, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Tropomyosin 1 deficiency facilitates cell state transitions and enhances hemogenic endothelial cell specification during hematopoiesis."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Stem Cell Reports (2024)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1016/j.stemcr.2024.08.001"}], "href": "https://doi.org/10.1016/j.stemcr.2024.08.001"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "39214082"}], "href": "https://pubmed.ncbi.nlm.nih.gov/39214082"}]}]}]}
NCBI Gene ID 100847033
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Predicted Functions View MIR4436B2's ARCHS4 Predicted Functions.
Co-expressed Genes View MIR4436B2's ARCHS4 Predicted Functions.
Expression in Tissues and Cell Lines View MIR4436B2's ARCHS4 Predicted Functions.

Functional Associations

MIR4436B2 has 93 functional associations with biological entities spanning 1 categories (cell line, cell type or tissue) extracted from 1 datasets.

Click the + buttons to view associations for MIR4436B2 from the datasets below.

If available, associations are ranked by standardized value

Dataset Summary
Klijn et al., Nat. Biotechnol., 2015 Cell Line Gene CNV Profiles cell lines with high or low copy number of MIR4436B2 gene relative to other cell lines from the Klijn et al., Nat. Biotechnol., 2015 Cell Line Gene CNV Profiles dataset.