| HGNC Family | Non-coding RNAs |
| Name | microRNA 6075 |
| 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 |
{"type": "root", "children": [{"type": "p", "children": [{"type": "t", "text": "\nAlthough none of the provided studies directly interrogate MIR6075, the collective evidence delineates a regulatory network in which secretory granule biogenesis and neuroendocrine differentiation are orchestrated by key signaling pathways and granin proteins. For example, activation of the receptor for advanced glycation end products (RAGE) by amphoterin initiates a CREB‐dependent gene expression program that upregulates chromogranins A and B during neuronal differentiation, while complementary experiments in non‐neuroendocrine cells demonstrate that elevated chromogranin B levels can markedly enhance the formation of dense core secretory granules."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "1"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nIn addition to their established roles in vesicle biogenesis, chromogranin proteins critically modulate intracellular calcium dynamics by interacting with the inositol 1,4,5‐trisphosphate receptor, and even localize to the nucleus where they regulate transcription of multiple target genes. These multifaceted functions underscore a cellular milieu in which fine‐tuning by regulatory RNAs is likely to be essential. In this context, MIR6075 may serve as a modulatory molecule that targets transcripts encoding key components of both the secretory apparatus and calcium signaling machinery, thereby influencing gene expression programs and cell functionality."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "3", "end_ref": "7"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nFurther support for the physiological importance of this regulatory axis is derived from animal models deficient in chromogranin expression. Such models exhibit impaired hormone release, reduced catecholamine storage in secretory vesicles, and alterations in stress responsiveness, metabolism, and even behavior. These observations suggest that the precise regulation of secretory granule formation and function is critical for proper neuronal and endocrine performance, and raise the intriguing possibility that MIR6075 could contribute to these processes by modulating the expression and activity of granin proteins and associated factors. In this way, MIR6075 might act as a fine‐tuner of vesicle biogenesis, calcium signaling, and transcriptional control, ultimately impacting neuroendocrine cell physiology."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "8", "end_ref": "13"}]}, {"type": "t", "text": "\n"}]}, {"type": "rg", "children": [{"type": "r", "ref": 1, "children": [{"type": "t", "text": "Henri J Huttunen, Juha Kuja-Panula, Heikki Rauvala "}, {"type": "b", "children": [{"type": "t", "text": "Receptor for advanced glycation end products (RAGE) signaling induces CREB-dependent chromogranin expression during neuronal differentiation."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "J Biol Chem (2002)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1074/jbc.M202515200"}], "href": "https://doi.org/10.1074/jbc.M202515200"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "12167613"}], "href": "https://pubmed.ncbi.nlm.nih.gov/12167613"}]}, {"type": "r", "ref": 2, "children": [{"type": "t", "text": "Yang Hoon Huh, Soung Hoo Jeon, Seung Hyun Yoo "}, {"type": "b", "children": [{"type": "t", "text": "Chromogranin B-induced secretory granule biogenesis: comparison with the similar role of chromogranin A."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "J Biol Chem (2003)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1074/jbc.M304942200"}], "href": "https://doi.org/10.1074/jbc.M304942200"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "12902350"}], "href": "https://pubmed.ncbi.nlm.nih.gov/12902350"}]}, {"type": "r", "ref": 3, "children": [{"type": "t", "text": "Seung Hyun Yoo, Soon Hee You, Moon Kyung Kang, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Localization of the secretory granule marker protein chromogranin B in the nucleus. Potential role in transcription control."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "J Biol Chem (2002)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1074/jbc.M105594200"}], "href": "https://doi.org/10.1074/jbc.M105594200"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "11854265"}], "href": "https://pubmed.ncbi.nlm.nih.gov/11854265"}]}, {"type": "r", "ref": 4, "children": [{"type": "t", "text": "Edwin C Thrower, Chi Un Choe, Seung Ho So, et al. "}, {"type": "b", "children": [{"type": "t", "text": "A functional interaction between chromogranin B and the inositol 1,4,5-trisphosphate receptor/Ca2+ channel."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "J Biol Chem (2003)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1074/jbc.M309307200"}], "href": "https://doi.org/10.1074/jbc.M309307200"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "14506248"}], "href": "https://pubmed.ncbi.nlm.nih.gov/14506248"}]}, {"type": "r", "ref": 5, "children": [{"type": "t", "text": "Stefan Schmidt, Michelle Mo, Felix M Heidrich, et al. "}, {"type": "b", "children": [{"type": "t", "text": "C-terminal domain of chromogranin B regulates intracellular calcium signaling."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "J Biol Chem (2011)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1074/jbc.M111.251330"}], "href": "https://doi.org/10.1074/jbc.M111.251330"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "22016391"}], "href": "https://pubmed.ncbi.nlm.nih.gov/22016391"}]}, {"type": "r", "ref": 6, "children": [{"type": "t", "text": "Natalia Domínguez, Judith Estévez-Herrera, Marta R Pardo, et al. "}, {"type": "b", "children": [{"type": "t", "text": "The functional role of chromogranins in exocytosis."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "J Mol Neurosci (2012)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1007/s12031-012-9736-2"}], "href": "https://doi.org/10.1007/s12031-012-9736-2"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "22415354"}], "href": "https://pubmed.ncbi.nlm.nih.gov/22415354"}]}, {"type": "r", "ref": 7, "children": [{"type": "t", "text": "Jésica Díaz-Vera, Marcial Camacho, José David Machado, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Chromogranins A and B are key proteins in amine accumulation, but the catecholamine secretory pathway is conserved without them."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "FASEB J (2012)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1096/fj.11-181941"}], "href": "https://doi.org/10.1096/fj.11-181941"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "21990378"}], "href": "https://pubmed.ncbi.nlm.nih.gov/21990378"}]}, {"type": "r", "ref": 8, "children": [{"type": "t", "text": "Nitish R Mahapatra, Manjula Mahata, Sajalendu Ghosh, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Molecular basis of neuroendocrine cell type-specific expression of the chromogranin B gene: Crucial role of the transcription factors CREB, AP-2, Egr-1 and Sp1."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "J Neurochem (2006)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1111/j.1471-4159.2006.04128.x"}], "href": "https://doi.org/10.1111/j.1471-4159.2006.04128.x"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "16987240"}], "href": "https://pubmed.ncbi.nlm.nih.gov/16987240"}]}, {"type": "r", "ref": 9, "children": [{"type": "t", "text": "Anna Nilsson, Maria Fälth, Xiaoqun Zhang, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Striatal alterations of secretogranin-1, somatostatin, prodynorphin, and cholecystokinin peptides in an experimental mouse model of Parkinson disease."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Mol Cell Proteomics (2009)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1074/mcp.M800454-MCP200"}], "href": "https://doi.org/10.1074/mcp.M800454-MCP200"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "19131325"}], "href": "https://pubmed.ncbi.nlm.nih.gov/19131325"}]}, {"type": "r", "ref": 10, "children": [{"type": "t", "text": "Jésica Díaz-Vera, Yézer G Morales, Juan R Hernández-Fernaud, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Chromogranin B gene ablation reduces the catecholamine cargo and decelerates exocytosis in chromaffin secretory vesicles."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "J Neurosci (2010)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1523/JNEUROSCI.2894-09.2010"}], "href": "https://doi.org/10.1523/JNEUROSCI.2894-09.2010"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "20089903"}], "href": "https://pubmed.ncbi.nlm.nih.gov/20089903"}]}, {"type": "r", "ref": 11, "children": [{"type": "t", "text": "Stefanie Obermüller, Federico Calegari, Angus King, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Defective secretion of islet hormones in chromogranin-B deficient mice."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "PLoS One (2010)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1371/journal.pone.0008936"}], "href": "https://doi.org/10.1371/journal.pone.0008936"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "20126668"}], "href": "https://pubmed.ncbi.nlm.nih.gov/20126668"}]}, {"type": "r", "ref": 12, "children": [{"type": "t", "text": "Daniel Pereda, Marta R Pardo, Yezer Morales, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Mice lacking chromogranins exhibit increased aggressive and depression-like behaviour."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Behav Brain Res (2015)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1016/j.bbr.2014.09.022"}], "href": "https://doi.org/10.1016/j.bbr.2014.09.022"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "25257107"}], "href": "https://pubmed.ncbi.nlm.nih.gov/25257107"}]}, {"type": "r", "ref": 13, "children": [{"type": "t", "text": "Natalia Dominguez, Jan R T van Weering, Ricardo Borges, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Dense-core vesicle biogenesis and exocytosis in neurons lacking chromogranins A and B."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "J Neurochem (2018)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1111/jnc.14263"}], "href": "https://doi.org/10.1111/jnc.14263"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "29178418"}], "href": "https://pubmed.ncbi.nlm.nih.gov/29178418"}]}]}]}
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| Synonyms | HSA-MIR-6075 |
| NCBI Gene ID | 102466103 |
| API | |
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| Predicted Functions |
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| Co-expressed Genes |
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| Expression in Tissues and Cell Lines |
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MIR6075 has 0 functional associations with biological entities spanning 0 categories () extracted from 0 datasets.
Click the + buttons to view associations for MIR6075 from the datasets below.
If available, associations are ranked by standardized value
| Dataset | Summary |
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