| HGNC Family | Non-coding RNAs |
| Name | microRNA 3616 |
| 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": "\nMIR3616, whose function is intertwined with autophagic regulation, has been shown to modulate the activity of key Beclin 1–Vps34 complexes. In this context, MIR3616 functions as a negative regulator of autophagic flux by interacting with subunits of the autophagy‐initiating complex, thereby controlling both the formation of autophagosomes and their maturation. In cellular systems, distinct complexes containing Beclin 1 have been identified—some that promote autophagy (via partners such as Atg14L) and others that, through association with proteins like Rubicon, downregulate the lipid kinase activity of Vps34 and impair autophagosome maturation."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "1", "end_ref": "5"}]}, {"type": "t", "text": ""}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nBeyond its canonical role in autophagosome regulation, MIR3616 exerts tissue‐ and context‐specific effects. For example, an age‐dependent increase in its inhibitory function has been correlated with declines in autophagy that contribute to cellular senescence and reduced healthspan, whereas in certain settings, such as myocardial ischemia/reperfusion injury, upregulation of MIR3616 is associated with aberrant accumulation of autophagosomes and a form of cell death termed “autosis.” In diverse tissues—including pancreatic β cells, podocytes, and retinal pigment epithelial cells—MIR3616 modulates stress responses by influencing downstream signaling pathways such as EGFR and by interacting with key regulators of immune responses (e.g., interference with IRF3 dimerization to restrain type I interferon signaling)."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "6", "end_ref": "11"}]}, {"type": "t", "text": ""}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nIn addition, MIR3616 contributes to the regulation of specialized cellular functions. In the reproductive system, for instance, its suppression of excessive autophagy within Sertoli cells is critical for maintaining spermatogenesis and the proper expression of cell‐supportive transcription factors. In adipocytes and hepatocytes, MIR3616 activity has been linked to metabolic adaptations during fasting, influencing lipid mobilization and lipophagy that modulate systemic energy balance. Furthermore, in the heart, by ensuring proper recycling of key receptors, MIR3616 provides protection against pressure overload, while in liver and kidney settings it affects the progression of inflammatory and fibrotic responses. Collectively, these studies underscore the diverse and context‐dependent functions of MIR3616 in controlling autophagic flux, mediating stress responses, and maintaining cellular and tissue homeostasis."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "12", "end_ref": "18"}]}, {"type": "t", "text": ""}]}, {"type": "rg", "children": [{"type": "r", "ref": 1, "children": [{"type": "t", "text": "Yun Zhong, Qing Jun Wang, Xianting Li, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Distinct regulation of autophagic activity by Atg14L and Rubicon associated with Beclin 1-phosphatidylinositol-3-kinase complex."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Nat Cell Biol (2009)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1038/ncb1854"}], "href": "https://doi.org/10.1038/ncb1854"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "19270693"}], "href": "https://pubmed.ncbi.nlm.nih.gov/19270693"}]}, {"type": "r", "ref": 2, "children": [{"type": "t", "text": "Kohichi Matsunaga, Tatsuya Saitoh, Keisuke Tabata, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Two Beclin 1-binding proteins, Atg14L and Rubicon, reciprocally regulate autophagy at different stages."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Nat Cell Biol (2009)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1038/ncb1846"}], "href": "https://doi.org/10.1038/ncb1846"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "19270696"}], "href": "https://pubmed.ncbi.nlm.nih.gov/19270696"}]}, {"type": "r", "ref": 3, "children": [{"type": "t", "text": "Zhenguo Zi, Zongpei Song, Shasha Zhang, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Rubicon deficiency enhances cardiac autophagy and protects mice from lipopolysaccharide-induced lethality and reduction in stroke volume."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "J Cardiovasc Pharmacol (2015)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1097/FJC.0000000000000188"}], "href": "https://doi.org/10.1097/FJC.0000000000000188"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "25502307"}], "href": "https://pubmed.ncbi.nlm.nih.gov/25502307"}]}, {"type": "r", "ref": 4, "children": [{"type": "t", "text": "Jae-Hoon Kim, Tae-Hwan Kim, Hyun-Cheol Lee, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Rubicon Modulates Antiviral Type I Interferon (IFN) Signaling by Targeting IFN Regulatory Factor 3 Dimerization."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "J Virol (2017)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1128/JVI.00248-17"}], "href": "https://doi.org/10.1128/JVI.00248-17"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "28468885"}], "href": "https://pubmed.ncbi.nlm.nih.gov/28468885"}]}, {"type": "r", "ref": 5, "children": [{"type": "t", "text": "Luis Muniz-Feliciano, Teresa A Doggett, Zhenqing Zhou, et al. "}, {"type": "b", "children": [{"type": "t", "text": "RUBCN/rubicon and EGFR regulate lysosomal degradative processes in the retinal pigment epithelium (RPE) of the eye."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Autophagy (2017)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1080/15548627.2017.1380124"}], "href": "https://doi.org/10.1080/15548627.2017.1380124"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "28933590"}], "href": "https://pubmed.ncbi.nlm.nih.gov/28933590"}]}, {"type": "r", "ref": 6, "children": [{"type": "t", "text": "Shuhei Nakamura, Masaki Oba, Mari Suzuki, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Suppression of autophagic activity by Rubicon is a signature of aging."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Nat Commun (2019)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1038/s41467-019-08729-6"}], "href": "https://doi.org/10.1038/s41467-019-08729-6"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "30783089"}], "href": "https://pubmed.ncbi.nlm.nih.gov/30783089"}]}, {"type": "r", "ref": 7, "children": [{"type": "t", "text": "Jihoon Nah, Peiyong Zhai, Chun-Yang Huang, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Upregulation of Rubicon promotes autosis during myocardial ischemia/reperfusion injury."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "J Clin Invest (2020)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1172/JCI132366"}], "href": "https://doi.org/10.1172/JCI132366"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "32364533"}], "href": "https://pubmed.ncbi.nlm.nih.gov/32364533"}]}, {"type": "r", "ref": 8, "children": [{"type": "t", "text": "Shuhei Aoyama, Yuya Nishida, Yoshio Fujitani, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Rubicon in pancreatic beta cells plays a limited role in maintaining glucose homeostasis following increased insulin resistance."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Endocr J (2020)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1507/endocrj.EJ20-0326"}], "href": "https://doi.org/10.1507/endocrj.EJ20-0326"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "32669482"}], "href": "https://pubmed.ncbi.nlm.nih.gov/32669482"}]}, {"type": "r", "ref": 9, "children": [{"type": "t", "text": "Tadashi Yamamuro, Tsuyoshi Kawabata, Atsunori Fukuhara, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Age-dependent loss of adipose Rubicon promotes metabolic disorders via excess autophagy."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Nat Commun (2020)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1038/s41467-020-17985-w"}], "href": "https://doi.org/10.1038/s41467-020-17985-w"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "32811819"}], "href": "https://pubmed.ncbi.nlm.nih.gov/32811819"}]}, {"type": "r", "ref": 10, "children": [{"type": "t", "text": "Yan Li, Yu Pan, Shirong Cao, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Podocyte EGFR Inhibits Autophagy Through Upregulation of Rubicon in Type 2 Diabetic Nephropathy."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Diabetes (2021)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.2337/db20-0660"}], "href": "https://doi.org/10.2337/db20-0660"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "33239448"}], "href": "https://pubmed.ncbi.nlm.nih.gov/33239448"}]}, {"type": "r", "ref": 11, "children": [{"type": "t", "text": "Satoru Ando, Noriyasu Hashida, Daisuke Yamashita, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Rubicon regulates A2E-induced autophagy impairment in the retinal pigment epithelium implicated in the pathology of age-related macular degeneration."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Biochem Biophys Res Commun (2021)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1016/j.bbrc.2021.02.148"}], "href": "https://doi.org/10.1016/j.bbrc.2021.02.148"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "33740621"}], "href": "https://pubmed.ncbi.nlm.nih.gov/33740621"}]}, {"type": "r", "ref": 12, "children": [{"type": "t", "text": "Tadashi Yamamuro, Shuhei Nakamura, Yu Yamano, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Rubicon prevents autophagic degradation of GATA4 to promote Sertoli cell function."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "PLoS Genet (2021)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1371/journal.pgen.1009688"}], "href": "https://doi.org/10.1371/journal.pgen.1009688"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "34351902"}], "href": "https://pubmed.ncbi.nlm.nih.gov/34351902"}]}, {"type": "r", "ref": 13, "children": [{"type": "t", "text": "Yasuhiro Akazawa, Manabu Taneike, Hiromichi Ueda, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Rubicon-regulated beta-1 adrenergic receptor recycling protects the heart from pressure overload."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Sci Rep (2022)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1038/s41598-021-03920-6"}], "href": "https://doi.org/10.1038/s41598-021-03920-6"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "34996972"}], "href": "https://pubmed.ncbi.nlm.nih.gov/34996972"}]}, {"type": "r", "ref": 14, "children": [{"type": "t", "text": "Tadashi Yamamuro, Shuhei Nakamura, Kyosuke Yanagawa, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Loss of RUBCN/rubicon in adipocytes mediates the upregulation of autophagy to promote the fasting response."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Autophagy (2022)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1080/15548627.2022.2047341"}], "href": "https://doi.org/10.1080/15548627.2022.2047341"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "35282767"}], "href": "https://pubmed.ncbi.nlm.nih.gov/35282767"}]}, {"type": "r", "ref": 15, "children": [{"type": "t", "text": "Yajun Chen, Yiping He, Xinyi Wu, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Rubicon promotes the M2 polarization of Kupffer cells via LC3-associated phagocytosis-mediated clearance to improve liver transplantation."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Cell Immunol (2022)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1016/j.cellimm.2022.104556"}], "href": "https://doi.org/10.1016/j.cellimm.2022.104556"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "35700602"}], "href": "https://pubmed.ncbi.nlm.nih.gov/35700602"}]}, {"type": "r", "ref": 16, "children": [{"type": "t", "text": "Shiyao Liao, Qiangqiang Zheng, Haotian Shen, et al. "}, {"type": "b", "children": [{"type": "t", "text": "HECTD1-Mediated Ubiquitination and Degradation of Rubicon Regulates Autophagy and Osteoarthritis Pathogenesis."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Arthritis Rheumatol (2023)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1002/art.42369"}], "href": "https://doi.org/10.1002/art.42369"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "36121967"}], "href": "https://pubmed.ncbi.nlm.nih.gov/36121967"}]}, {"type": "r", "ref": 17, "children": [{"type": "t", "text": "Yayong Li, Yuanguo Chen, Xiao Xiao, et al. "}, {"type": "b", "children": [{"type": "t", "text": "CX3CL1 represses autophagy via CX3CR1/ CaMKIIδ/HDAC4/Rubicon axis and exacerbates chronic intermittent hypoxia induced Kupffer cell apoptosis."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Cell Signal (2023)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1016/j.cellsig.2023.110873"}], "href": "https://doi.org/10.1016/j.cellsig.2023.110873"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "37640194"}], "href": "https://pubmed.ncbi.nlm.nih.gov/37640194"}]}, {"type": "r", "ref": 18, "children": [{"type": "t", "text": "Anh The Nguyen, Masashi Masuda, Yuki Mori, et al. "}, {"type": "b", "children": [{"type": "t", "text": "All-trans retinoic acid induces lipophagy by reducing Rubicon in Hepa1c1c7 cells."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "J Lipid Res (2024)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1016/j.jlr.2024.100598"}], "href": "https://doi.org/10.1016/j.jlr.2024.100598"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "39032560"}], "href": "https://pubmed.ncbi.nlm.nih.gov/39032560"}]}]}]}
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| Synonyms | MIR-3616 |
| NCBI Gene ID | 100500814 |
| 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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MIR3616 has 265 functional associations with biological entities spanning 3 categories (molecular profile, cell line, cell type or tissue, gene, protein or microRNA) extracted from 11 datasets.
Click the + buttons to view associations for MIR3616 from the datasets below.
If available, associations are ranked by standardized value
| Dataset | Summary | |
|---|---|---|
| CCLE Cell Line Gene CNV Profiles | cell lines with high or low copy number of MIR3616 gene relative to other cell lines from the CCLE Cell Line Gene CNV Profiles dataset. | |
| COSMIC Cell Line Gene CNV Profiles | cell lines with high or low copy number of MIR3616 gene relative to other cell lines from the COSMIC Cell Line Gene CNV Profiles dataset. | |
| ENCODE Histone Modification Site Profiles | histone modification site profiles with high histone modification abundance at MIR3616 gene from the ENCODE Histone Modification Site Profiles dataset. | |
| ENCODE Transcription Factor Binding Site Profiles | transcription factor binding site profiles with transcription factor binding evidence at the promoter of MIR3616 gene from the ENCODE Transcription Factor Binding Site Profiles dataset. | |
| ENCODE Transcription Factor Targets | transcription factors binding the promoter of MIR3616 gene in ChIP-seq datasets from the ENCODE Transcription Factor Targets dataset. | |
| GTEx Tissue Gene Expression Profiles | tissues with high or low expression of MIR3616 gene relative to other tissues from the GTEx Tissue Gene Expression Profiles dataset. | |
| JASPAR Predicted Transcription Factor Targets | transcription factors regulating expression of MIR3616 gene predicted using known transcription factor binding site motifs from the JASPAR Predicted Transcription Factor Targets dataset. | |
| Klijn et al., Nat. Biotechnol., 2015 Cell Line Gene CNV Profiles | cell lines with high or low copy number of MIR3616 gene relative to other cell lines from the Klijn et al., Nat. Biotechnol., 2015 Cell Line Gene CNV Profiles dataset. | |
| KnockTF Gene Expression Profiles with Transcription Factor Perturbations | transcription factor perturbations changing expression of MIR3616 gene from the KnockTF Gene Expression Profiles with Transcription Factor Perturbations dataset. | |
| MotifMap Predicted Transcription Factor Targets | transcription factors regulating expression of MIR3616 gene predicted using known transcription factor binding site motifs from the MotifMap Predicted Transcription Factor Targets dataset. | |
| Roadmap Epigenomics Histone Modification Site Profiles | histone modification site profiles with high histone modification abundance at MIR3616 gene from the Roadmap Epigenomics Histone Modification Site Profiles dataset. | |