Affinage

MIA3

Transport and Golgi organization protein 1 homolog · UniProt Q5JRA6

Length
1907 aa
Mass
213.7 kDa
Annotated
2026-06-10
100 papers in source corpus 23 papers cited in narrative 22 extracted findings
Cross-family judge vs UniProt: Affinage preferred faithfulness: 7/7 claims corpus-supported (100%)

Mechanistic narrative

Synthesis pass · prose summary of the discoveries below

MIA3 (TANGO1) is an integral ER exit site transmembrane protein that acts as the master scaffold organizing the export of bulky secretory cargo from the endoplasmic reticulum (PMID:19269366, PMID:29513218). It is structurally bifunctional: a luminal SH3-like domain captures cargoes including collagen VII, procollagens, and ApoB-lipoproteins, while its cytoplasmic proline-rich domain (PRD) binds the COPII inner coat subunit Sec23/24 through repeated PPP motifs, allowing a single receptor to nucleate accretion of multiple inner-coat copies into the helical lattice needed to build large carriers, with TANGO1 itself excluded from the budding vesicle (PMID:19269366, PMID:27551091). At ER exit sites TANGO1 assembles into a ring through radial contacts with COPII and lateral self- and co-receptor interactions with cTAGE5 and the short isoform TANGO1S, and it anchors the export machinery via direct binding to Sec16, organizing functional ER exit sites and recruiting cTAGE5/Sec12 complexes (PMID:29513218, PMID:21525241, PMID:28442536). Ring assembly couples anterograde cargo export to retrograde membrane flow: TANGO1's first coiled-coil recruits ERGIC membranes through the NRZ (NBAS/RINT1/ZW10) tether and a SNARE set (Syntaxin 18, BNIP1, USE1, YKT6), supplying membrane to elongate procollagen-sized carriers, and its membrane helices reduce lipid diffusion to act as a barrier preventing ER–ERGIC mixing (PMID:26568311, PMID:29513218, PMID:33169667, PMID:32452385). Cargo selectivity is modular—ApoB-lipoprotein export additionally requires the TALI co-receptor whereas procollagen XII does not (PMID:27138255)—and ER exit site assembly is dynamically controlled by CK1 phosphorylation, which dissociates TANGO1 from Sec16 to drive disassembly during mitosis, counteracted by PP1 (PMID:32818468). Loss of TANGO1 in mice causes broad collagen secretion failure, UPR induction, skeletal defects, and neonatal lethality, and in human cells disrupts secretory pathway organization at the ER-Golgi interface for cargo of all sizes (PMID:21606205, PMID:34350936). Biallelic TANGO1 mutations cause a syndromal human disease with dentinogenesis imperfecta, short stature, skeletal abnormalities, diabetes, hearing loss, and intellectual disability, with the truncated protein dispersed from ER exit sites and acting dominant-negatively on collagen I secretion (PMID:32101163).

Mechanistic history

Synthesis pass · year-by-year structured walk · 14 steps
  1. 2006 Medium

    Before its secretory role was known, MIA3 was characterized as a tumor suppressor controlling cell migration, establishing the first functional link for the gene.

    Evidence RT-PCR, IHC, gain/loss-of-function migration assays in melanoma cells

    PMID:17044017

    Open questions at the time
    • No molecular mechanism connecting MIA3 to migration
    • Relationship to its later-defined secretory function not addressed
  2. 2007 Low

    An early candidate partner (leukocyte integrin CD11c) was identified, framing MIA3 as a modulator of integrin-mediated adhesion before its ER role emerged.

    Evidence Affinity pulldown/MS, recombinant protein adhesion and migration assays

    PMID:17726152

    Open questions at the time
    • Single pulldown without reciprocal validation
    • Mechanism of integrin modulation proposed but not established
    • Hard to reconcile with intracellular ER exit site localization
  3. 2009 High

    The foundational study defined TANGO1 as an ER exit site transmembrane cargo receptor with a luminal collagen-binding SH3 domain and a cytoplasmic PRD that engages COPII, answering how bulky collagen VII is loaded into carriers while the receptor stays behind.

    Evidence Genome-wide screen, fractionation/imaging, domain binding assays, siRNA with collagen secretion readout

    PMID:19269366

    Open questions at the time
    • Mechanism of carrier enlargement not resolved
    • Generality across collagen types untested
  4. 2011 High

    Knockout mice and identification of cTAGE5 as a co-receptor established that Mia3 is broadly required for secretion of all collagens and acts within a multiprotein receptor complex at ER exit sites.

    Evidence Knockout mouse with histology and collagen assays; reciprocal Co-IP and domain mapping for cTAGE5

    PMID:21525241 PMID:21606205

    Open questions at the time
    • How membrane is supplied for large carriers unknown
    • Stoichiometry of the TANGO1/cTAGE5/COPII assembly unresolved
  5. 2015 High

    Identification of NRZ-dependent ERGIC membrane recruitment and the required SNARE set explained how TANGO1 supplies membrane to grow procollagen-sized carriers.

    Evidence siRNA, mitochondrial retargeting of the first coiled-coil, live imaging, SNARE identification

    PMID:26568311

    Open questions at the time
    • Spatial coordination of fusion with bud growth not resolved
    • Whether membrane addition drives elongation directly untested at this stage
  6. 2016 High

    Multiple studies resolved the receptor's molecular architecture—atomic PRD-Sec23 PPP-motif binding, ring assembly coupled to NRZ-dependent retrograde flow, isoform complexes, and cargo-specific co-receptors—converting TANGO1 from a cargo receptor into an organizing scaffold of ER exit sites.

    Evidence X-ray crystallography with mutagenesis; super-resolution imaging and Co-IP for ring/NRZ; native gel and gel filtration for isoform complexes; Co-IP and cargo-specific secretion assays for TALI/ApoB

    PMID:27138255 PMID:27413011 PMID:27551091 PMID:29513218

    Open questions at the time
    • Functional distinction between TANGO1L and TANGO1S incompletely defined
    • How ring geometry sets carrier size not directly measured
  7. 2016 High

    TANGO1 was placed in a physiological circuit: TGFβ/XBP1-driven UPR upregulates it in hepatic stellate cells to support collagen I secretion, linking the receptor to fibrosis.

    Evidence siRNA, UPR reporters, XBP1 ChIP/overexpression, heterozygous KO mouse fibrosis models

    PMID:28039913

    Open questions at the time
    • Direct XBP1 binding to the MIA3 promoter not atomically mapped
    • Therapeutic targeting consequences not established
  8. 2017 High

    Direct binding to Sec16 and conserved Drosophila genetics established TANGO1 as an ER exit site organizer that couples ERES to Golgi and maintains organelle architecture independent of bulky cargo transport.

    Evidence Co-IP with mitochondrial retargeting rescue; Drosophila loss/gain-of-function with multi-cargo secretion assays and double-mutant epistasis

    PMID:28280122 PMID:28442536 PMID:29138315

    Open questions at the time
    • Molecular basis of the secretion-independent architectural role undefined
    • How Sec16 binding integrates with COPII assembly mechanistically unresolved
  9. 2017 Medium

    An upstream regulatory axis was defined in endothelium, where ADTRP via PIK3R3-AKT controls MIA3 expression to govern monocyte adhesion and transendothelial migration.

    Evidence siRNA, constitutively active AKT1 and MIA3 overexpression rescue, endothelial functional assays

    PMID:28341552

    Open questions at the time
    • Single lab
    • Connection between secretory scaffolding function and endothelial adhesion phenotype unclear
  10. 2018 High

    Reconstitution showed TANGO1, procollagen I, cTAGE5 and SEC12 are co-packaged into large COPII carriers, with HSP47 RDEL-mediated COPI retrieval recycling TANGO1, and luminal targeting of SEC12 to cargo being sufficient to generate large carriers.

    Evidence Live imaging, fractionation, split-GFP reconstitution, siRNA

    PMID:30545919

    Open questions at the time
    • Quantitative contribution of SEC12 enrichment to carrier size in vivo unresolved
    • Generality to non-collagen bulky cargo untested
  11. 2020 Medium

    Biophysical modeling and reconstitution defined how the TANGO1 ring stabilizes the open bud neck as a linactant and how its membrane helices form a lipid diffusion barrier, providing a physical mechanism for large carrier formation.

    Evidence Theoretical modeling; lipid diffusion barrier reconstitution in model membranes

    PMID:32452385 PMID:33169667

    Open questions at the time
    • Theoretical elongation model not independently validated in cells
    • Diffusion barrier shown only in reconstituted membranes
  12. 2020 High

    A CK1/PP1 phospho-switch was shown to control ER exit site dynamics, explaining how secretion is shut down during mitosis through TANGO1-Sec16 dissociation.

    Evidence Phosphorylation assays, kinase/phosphatase inhibitors, phospho-TANGO1/Sec16 Co-IP, cell-cycle synchronization

    PMID:32818468

    Open questions at the time
    • Phosphosite mapping on TANGO1 not detailed
    • Whether the switch operates outside mitosis unaddressed
  13. 2020 High

    Human genetics established MIA3 as a disease gene: biallelic mutations cause a syndromal disorder via a dominant-negative truncated protein dispersed from ER exit sites.

    Evidence Whole-exome sequencing, mRNA/protein analysis, localization and collagen I secretion assays in cells

    PMID:32101163

    Open questions at the time
    • Genotype-phenotype range across patients limited
    • Tissue-specific basis of diverse symptoms unexplained
  14. 2021 High

    Isoform-specific human knockouts revealed TANGO1S as the functionally dominant isoform, required for ER-Golgi intermediate compartment organization and secretion of cargo of all sizes, broadening TANGO1's role beyond bulky cargo.

    Evidence CRISPR isoform-specific KOs, light/electron microscopy, proteomics, transcriptomics, secretion assays

    PMID:34350936

    Open questions at the time
    • Molecular basis for TANGO1S sufficiency over TANGO1L undefined
    • Why small-cargo secretion depends on TANGO1 mechanistically unresolved

Open questions

Synthesis pass · forward-looking unresolved questions
  • How TANGO1's atomically defined cargo-binding, COPII-scaffolding, and membrane-fusion activities are integrated in real time to set carrier dimensions, and how its early adhesion/tumor-suppressor activities relate to its core ER export function, remain open.
  • No unified structural model of the assembled TANGO1 ring with cargo, COPII, and ERGIC membrane
  • Mechanistic link between secretory scaffolding and migration/adhesion phenotypes unestablished

Mechanism profile

Synthesis pass · controlled-vocabulary classification · explore literature graph →
Molecular activity
GO:0008092 cytoskeletal protein binding 3 GO:0038024 cargo receptor activity 3 GO:0060090 molecular adaptor activity 3
Localization
GO:0005783 endoplasmic reticulum 3
Pathway
R-HSA-392499 Metabolism of proteins 3 R-HSA-5653656 Vesicle-mediated transport 3 R-HSA-9609507 Protein localization 3
Partners
CTAGE5HSP47SEC12SEC16SEC23STX18TALIYKT6
Complex memberships
NRZ tether (NBAS/RINT1/ZW10) - associatedTANGO1 ring at ER exit sitesTANGO1L/cTAGE5/Sec12 (~900 kDa)TANGO1S/cTAGE5/Sec12 (~700 kDa)

Evidence

Reading pass · 22 per-paper findings extracted from the source corpus
Year Finding Method Journal Conf PMIDs
2009 TANGO1 (MIA3) is an integral membrane protein localized to ER exit sites with a luminal SH3 domain that binds collagen VII cargo and a cytoplasmic proline-rich domain (PRD) that binds COPII coat subunits Sec23/24, positioning it to load bulky collagen VII into growing COPII carriers while itself remaining excluded from the budding vesicle. Genome-wide screen, subcellular fractionation/localization, domain binding assays (SH3-collagen VII interaction, PRD-Sec23/24 interaction), siRNA knockdown with collagen secretion readout Cell High 19269366
2011 Mia3/TANGO1 knockout mice show defective secretion of numerous collagens (I, II, III, IV, VII, IX) from multiple cell types (chondrocytes, fibroblasts, endothelial cells), intracellular collagen accumulation, unfolded protein response induction, impaired chondrocyte maturation and bone mineralization, dwarfism, and neonatal lethality, establishing that Mia3 is broadly required for efficient secretion of all collagen molecules. Knockout mouse model, immunofluorescence, Western blot, collagen secretion assays from primary cells, histology, skeletal phenotyping The Journal of cell biology High 21606205
2011 cTAGE5 forms a complex with TANGO1 at ER exit sites through coiled-coil domain interactions; both proteins interact with COPII Sec23/24 via their C-terminal proline-rich domains and are both required for collagen VII secretion, with cTAGE5 acting as a co-receptor of TANGO1. Co-immunoprecipitation, localization (confocal microscopy), domain mapping, siRNA knockdown with collagen secretion assay Molecular biology of the cell High 21525241
2015 TANGO1 recruits YKT6-containing ERGIC membranes to procollagen VII-enriched ER exit site patches; the full complement of SNAREs required for this ERGIC membrane fusion includes t-SNAREs Syntaxin 18, BNIP1, and USE1, and v-SNARE YKT6. The first coiled-coil domain (residues 1214–1396) of TANGO1 is sufficient to recruit ERGIC membranes even when artificially retargeted to mitochondria. siRNA knockdown, domain-targeting experiments (mitochondrial retargeting), live imaging, SNARE identification eLife High 26568311
2016 TANGO1 assembles into a ring at ER exit sites organized by radial interactions with COPII and lateral interactions with cTAGE5, TANGO1-short, or itself; TANGO1 recruits ERGIC membranes for collagen export via the NRZ (NBAS/RINT1/ZW10) tether complex, thereby coupling retrograde membrane flow to anterograde cargo transport. Without the NRZ complex, the TANGO1 ring does not assemble. Super-resolution microscopy, Co-IP, siRNA knockdown, domain interaction assays eLife High 29513218
2016 X-ray crystallography and biochemical analysis showed that TANGO1 and cTAGE5 proline-rich domains (PRDs) bind Sec23 via repeated PPP motifs, enabling a single TANGO1/cTAGE5 receptor to bind multiple copies of COPII inner coat protein in a close-packed array, promoting accretion of inner coat proteins into a helical lattice for large COPII carrier formation. X-ray crystallography, biochemical binding assays (ITC/pulldown), mutagenesis of PPP motifs Proceedings of the National Academy of Sciences of the United States of America High 27551091
2016 TANGO1 and TALI (a chimeric MIA2/cTAGE5 protein) together bind ApoB and are both required for recruitment of ApoB-containing lipid particles (pre-chylomicrons and pre-VLDLs) to ER exit sites and their export; procollagen XII export by the same cells requires only TANGO1, not TALI, indicating cargo-specific co-receptor requirements. Co-IP (TANGO1-TALI interaction; both with ApoB), siRNA knockdown, secretion assays (ApoB, procollagen XII) The Journal of cell biology High 27138255
2016 TANGO1 exists in two stable macromolecular complexes at ER exit sites: TANGO1L/cTAGE5/Sec12 (~900 kDa) and TANGO1S/cTAGE5/Sec12 (~700 kDa); TANGO1S lacks the luminal collagen-binding domain but is independently required for collagen export from the ER. The two isoforms are interchangeable for collagen export. Native gel electrophoresis, gel filtration, siRNA knockdown of individual isoforms, collagen secretion assay Molecular biology of the cell Medium 27413011
2016 The unfolded protein response (UPR) upregulates TANGO1 expression in hepatic stellate cells (HSCs) in response to TGFβ; this is mediated by the transcription factor XBP1. Depletion of TANGO1 in HSCs blocks collagen I secretion, causes procollagen I retention in the ER, induces the UPR, and leads to HSC apoptosis. TANGO1+/- mice show reduced hepatic fibrosis in CCl4 and bile duct ligation models. siRNA screen, siRNA knockdown, collagen secretion assay, UPR reporter assays, XBP1 ChIP/overexpression, heterozygous KO mouse models Hepatology (Baltimore, Md.) High 28039913
2017 TANGO1 directly interacts with Sec16, and this interaction is required for correct localization of TANGO1 isoforms and for organization of ER exit sites; depletion of TANGO1 disassembles COPII components and membrane-bound ER-resident complexes, reducing functional ER exit sites and delaying secretion. Ectopic expression of the TANGO1 C-terminal Sec16-binding domain in mitochondria recruits Sec16 and other COPII components. TANGO1 also recruits cTAGE5/Sec12-containing macromolecular complexes to ER exit sites. Co-IP (TANGO1-Sec16 interaction), mitochondrial retargeting assay, siRNA knockdown, confocal microscopy, secretion assays The Journal of cell biology High 28442536
2017 In Drosophila, Tango1 (the only MIA/cTAGE family member in flies) forms rings that hold COPII carriers and Golgi in close proximity at ER exit sites; loss of Tango1 reduces ERES size, causes ERES-Golgi uncoupling, and impairs secretion of collagen and all other tested cargoes. Overexpression of Tango1 creates more and larger ERESs, supporting an organizer role. Genetic loss-of-function (Drosophila mutants), live imaging, immunofluorescence, secretion assays for multiple cargo types The Journal of cell biology High 28280122
2017 In Drosophila, loss of Tango1 causes ER stress and defects in cell shape secondary to retention of bulky cargo (e.g., Dumpy); removal of bulky cargo from cells restores secretion of non-bulky proteins, cell morphology, and attenuates ER stress. However, ER/Golgi morphological defects persist in the absence of bulky cargo, establishing a secretion-independent role for Tango1 in ER/Golgi architecture maintenance. Drosophila genetic loss-of-function, double-mutant epistasis (removing bulky cargo in Tango1-depleted cells), confocal imaging, ER stress assays Proceedings of the National Academy of Sciences of the United States of America High 29138315
2018 TANGO1 is co-packaged with procollagen I (PC1), cTAGE5, and SEC12 into large COPII-coated carriers; TANGO1 is retrieved back to the ER by COPI via the C-terminal RDEL retrieval sequence of HSP47. SEC12, normally excluded from small COPII vesicles, is enriched around ER membranes and large COPII carriers containing PC1; a split-GFP system reconstituting TANGO1 luminal domain targeting of SEC12 to PC1 was sufficient to generate large PC1 carriers. Live-cell imaging, subcellular fractionation, split-GFP reconstitution assay, immunofluorescence, siRNA knockdown Proceedings of the National Academy of Sciences of the United States of America High 30545919
2019 In Drosophila salivary glands, Tango1 forms ring-like structures that mediate formation of COPII rings (not vesicles); these COPII rings act as docking sites for the cis-Golgi, and secretory mucins emerge from the Golgi side of the Tango1-COPII-Golgi complexes. Loss of Tango1 disrupts COPII ring formation, COPII-cis-Golgi association, mucin O-glycosylation, and secretory granule biogenesis. A Tango1 self-association domain essential for ring formation was identified. High-resolution fluorescence imaging (Drosophila larval salivary glands), genetic KO, domain mapping (self-association domain identification) The Journal of biological chemistry Medium 31690624
2020 Theoretical/biophysical modeling shows that the TANGO1 ring acts as a linactant to stabilize the open neck of a nascent COPII bud; elongation into a procollagen-sized transport intermediate is facilitated by relief of membrane tension (via TANGO1-mediated ERGIC membrane fusion) and force application. The two TANGO1 membrane helices (TM spanning helix and IM inner-leaflet helix) together reduce lipid diffusion at curved membrane regions (reconstituted in model membranes), suggesting a mechanism to prevent membrane mixing during collagen export. Theoretical biophysical modeling; lipid diffusion barrier reconstitution in model membranes (GUVs/supported bilayers) with TANGO1 membrane helices eLife / eLife Medium 32452385 33169667
2020 TANGO1 phosphorylation is regulated by kinase CK1 (which phosphorylates TANGO1 and reduces its binding to Sec16, leading to ER exit site disassembly) and phosphatase PP1 (which dephosphorylates TANGO1). During mitosis, PP1-mediated dephosphorylation of TANGO1 decreases, resulting in net TANGO1 phosphorylation, Sec16 dissociation, and ER exit site disassembly. Phosphorylation assays, kinase/phosphatase inhibitor treatments, Co-IP (phospho-TANGO1 vs. Sec16), cell-cycle synchronization, confocal microscopy Developmental cell High 32818468
2020 Biallelic TANGO1 mutations in humans (synonymous substitution causing exon 8 skipping and truncated protein) cause a syndromal disease with dentinogenesis imperfecta, short stature, skeletal abnormalities, diabetes, hearing loss, and intellectual disability. The truncated TANGO1 protein is dispersed in the ER (not at ER exit sites) and its expression impairs cellular collagen I secretion in cells with endogenous intact TANGO1, indicating dominant-negative activity. Whole-exome sequencing, mRNA/protein analysis, subcellular localization by fluorescence microscopy, collagen I secretion assay in transfected HeLa/U2OS cells eLife High 32101163
2021 Loss of both TANGO1 isoforms (TANGO1S and TANGO1L) in human cells causes major defects in secretory pathway organization including failure to maintain ERGIC53 and SURF4 localization to the ER-Golgi intermediate compartment, dramatic ultrastructural changes at the ER-Golgi interface, and impaired secretion of all secretory cargo types (large and small). Loss of TANGO1L alone has limited impact on procollagen secretion and secretory pathway organization, indicating TANGO1S is the functionally dominant isoform. CRISPR genome engineering of isoform-specific knockouts, light microscopy, electron microscopy, secretion assays, proteomics, transcriptomics Journal of cell science High 34350936
2014 In Drosophila, the O-glycosyltransferase PGANT4 glycosylates Tango1 and protects it from furin (Dfur2)-mediated proteolytic cleavage; loss of PGANT4 results in Tango1 cleavage, loss of secretory granules, and disrupted apical secretion. Overexpression of Tango1 or knockdown of Dfur2 rescues the secretory defects caused by PGANT4 loss. Drosophila genetics, mass spectrometry (glycosylation identification), rescue experiments (Tango1 overexpression, Dfur2 knockdown), in vivo secretion assays Proceedings of the National Academy of Sciences of the United States of America Medium 24799692
2006 TANGO (MIA3) protein expression is reduced or lost in melanoma cell lines and tumor samples; re-expression of TANGO reduces melanoma cell motility, while antisense-mediated loss of TANGO enhances migration, establishing TANGO as a tumor suppressor that negatively regulates cell migration. RT-PCR, immunohistochemistry, stable transfection (TANGO re-expression and antisense knockdown), migration/motility assays International journal of cancer Medium 17044017
2007 Recombinant TANGO (MIA3) protein interacts with the leukocyte integrin CD11c (αX/CD18) and reduces monocyte attachment to fibrinogen and ICAM-1 and to endothelial cells, while increasing the migration capacity of premonocytic cells. TANGO interaction with CD11c does not compete directly with ligand binding, suggesting modulation of integrin activity. Pulldown/affinity isolation of interacting proteins (mass spectrometry identification of CD11c), recombinant protein stimulation, attachment and migration functional assays Journal of leukocyte biology Low 17726152
2017 ADTRP positively regulates MIA3/TANGO1 expression via a PIK3R3-AKT signaling axis in endothelial cells; knockdown of ADTRP downregulates MIA3/TANGO1, while constitutively active AKT1 or MIA3/TANGO1 overexpression rescues endothelial cell functions (monocyte adhesion, transendothelial migration, proliferation, apoptosis) impaired by ADTRP knockdown. MIA3/TANGO1 knockdown itself promotes monocyte adhesion and transendothelial migration. siRNA knockdown, Western blot, constitutively active AKT1 rescue, overexpression, monocyte adhesion and transendothelial migration assays Biochimica et biophysica acta. Molecular basis of disease Medium 28341552

Source papers

Stage 0 corpus · 100 papers · ranked by NIH iCite citations
Year Title Journal Citations PMID
2005 The Akt-mTOR tango and its relevance to cancer. Cancer cell 658 16169463
2015 PRESTO-Tango as an open-source resource for interrogation of the druggable human GPCRome. Nature structural & molecular biology 613 25895059
2009 TANGO1 facilitates cargo loading at endoplasmic reticulum exit sites. Cell 307 19269366
2018 Neuroinflammation: Microglia and T Cells Get Ready to Tango. Frontiers in immunology 294 29422891
2016 It takes two to tango: NAD+ and sirtuins in aging/longevity control. NPJ aging and mechanisms of disease 294 28721271
2019 CD36 tango in cancer: signaling pathways and functions. Theranostics 291 31410189
2009 It takes two to tango: regulation of G proteins by dimerization. Nature reviews. Molecular cell biology 236 19424291
2017 Transsynaptic Mapping of Second-Order Taste Neurons in Flies by trans-Tango. Neuron 206 29107518
2008 FOXO-binding partners: it takes two to tango. Oncogene 180 18391971
2018 Two to Tango: Dialog between Immunity and Stem Cells in Health and Disease. Cell 175 30388451
2011 Global defects in collagen secretion in a Mia3/TANGO1 knockout mouse. The Journal of cell biology 165 21606205
1997 The Drosophila tango gene encodes a bHLH-PAS protein that is orthologous to mammalian Arnt and controls CNS midline and tracheal development. Development (Cambridge, England) 157 9409674
2011 cTAGE5 mediates collagen secretion through interaction with TANGO1 at endoplasmic reticulum exit sites. Molecular biology of the cell 142 21525241
2012 It takes two to tango: IκBs, the multifunctional partners of NF-κB. Immunological reviews 138 22435547
2022 Efficacy and Safety of Switching to Dolutegravir/Lamivudine Versus Continuing a Tenofovir Alafenamide-Based 3- or 4-Drug Regimen for Maintenance of Virologic Suppression in Adults Living With Human Immunodeficiency Virus Type 1: Results Through Week 144 From the Phase 3, Noninferiority TANGO Randomized Trial. Clinical infectious diseases : an official publication of the Infectious Diseases Society of America 123 35079789
2018 TANGO1 builds a machine for collagen export by recruiting and spatially organizing COPII, tethers and membranes. eLife 120 29513218
2014 Replication stress and cancer: it takes two to tango. Experimental cell research 109 25257608
2004 The TIMPs tango with MMPs and more in the central nervous system. Journal of neuroscience research 109 14689443
2016 Human longevity: Genetics or Lifestyle? It takes two to tango. Immunity & ageing : I & A 100 27053941
2002 Receptor dimerization in GH and erythropoietin action--it takes two to tango, but how? Endocrinology 97 11751584
1999 The spineless-aristapedia and tango bHLH-PAS proteins interact to control antennal and tarsal development in Drosophila. Development (Cambridge, England) 97 10433921
2016 TANGO1 and Mia2/cTAGE5 (TALI) cooperate to export bulky pre-chylomicrons/VLDLs from the endoplasmic reticulum. The Journal of cell biology 95 27138255
2009 HIV-1 RNA dimerization: It takes two to tango. AIDS reviews 95 19529749
2015 TANGO1 recruits ERGIC membranes to the endoplasmic reticulum for procollagen export. eLife 92 26568311
2016 TANGO1/cTAGE5 receptor as a polyvalent template for assembly of large COPII coats. Proceedings of the National Academy of Sciences of the United States of America 91 27551091
2017 Metabolism and TAM functions-it takes two to tango. The FEBS journal 90 29055087
2016 The unfolded protein response mediates fibrogenesis and collagen I secretion through regulating TANGO1 in mice. Hepatology (Baltimore, Md.) 89 28039913
2010 The acinar-ductal tango in the pathogenesis of acute pancreatitis. Gut 89 20876773
2005 CCN proteins and cancer: two to tango. Frontiers in bioscience : a journal and virtual library 87 15769600
2013 The exocrine pancreas: the acinar-ductal tango in physiology and pathophysiology. Reviews of physiology, biochemistry and pharmacology 86 23881310
2009 Antizyme and antizyme inhibitor, a regulatory tango. Cellular and molecular life sciences : CMLS 85 19399584
2019 Dysfunctional Immune Response in Acute-on-Chronic Liver Failure: It Takes Two to Tango. Frontiers in immunology 80 31118937
2017 Tango1 spatially organizes ER exit sites to control ER export. The Journal of cell biology 79 28280122
2017 TANGO1 recruits Sec16 to coordinately organize ER exit sites for efficient secretion. The Journal of cell biology 72 28442536
2009 It takes two to tango: the structure and function of LIM, RING, PHD and MYND domains. Current pharmaceutical design 71 19925420
2013 Taking two to tango: a role for ghrelin receptor heterodimerization in stress and reward. Frontiers in neuroscience 67 24009547
2021 Inhibition of RAF dimers: it takes two to tango. Biochemical Society transactions 59 33367512
2019 Circulating Tumor Cell-Neutrophil Tango along the Metastatic Process. Cancer research 59 31527091
2014 O-glycosylation regulates polarized secretion by modulating Tango1 stability. Proceedings of the National Academy of Sciences of the United States of America 59 24799692
2011 Twisted tango: brain tumor neurovascular interactions. Nature neuroscience 57 22030548
2020 Biallelic TANGO1 mutations cause a novel syndromal disease due to hampered cellular collagen secretion. eLife 55 32101163
2018 Immunomodulation of Tumor Vessels: It Takes Two to Tango. Trends in immunology 53 30153971
2020 Does it take two to tango? RING domain self-association and activity in TRIM E3 ubiquitin ligases. Biochemical Society transactions 50 33170204
2012 It takes two to tango: dimerisation of glucocorticoid receptor and its anti-inflammatory functions. Steroids 50 23127816
2016 Distinct isoform-specific complexes of TANGO1 cooperatively facilitate collagen secretion from the endoplasmic reticulum. Molecular biology of the cell 48 27413011
2020 eIF-Three to Tango: emerging functions of translation initiation factor eIF3 in protein synthesis and disease. Journal of molecular cell biology 47 32279082
2022 It Takes Two to Tango: IGF-I and TSH Receptors in Thyroid Eye Disease. The Journal of clinical endocrinology and metabolism 46 35167695
2020 Fused in Sarcoma (FUS) in DNA Repair: Tango with Poly(ADP-ribose) Polymerase 1 and Compartmentalisation of Damaged DNA. International journal of molecular sciences 46 32987654
2021 Targeted Augmentation of Nuclear Gene Output (TANGO) of Scn1a rescues parvalbumin interneuron excitability and reduces seizures in a mouse model of Dravet Syndrome. Brain research 45 34843701
2019 Two to Tango: Co-evolution of Hominid Natural Killer Cell Receptors and MHC. Frontiers in immunology 45 30837985
2017 Dual function for Tango1 in secretion of bulky cargo and in ER-Golgi morphology. Proceedings of the National Academy of Sciences of the United States of America 45 29138315
2022 Learning to tango with four (or more): the molecular basis of adaptation to polyploid meiosis. Plant reproduction 44 36149479
2020 It Takes Two to Tango: Endothelial TGFβ/BMP Signaling Crosstalk with Mechanobiology. Cells 42 32858894
2018 TANGO1 and SEC12 are copackaged with procollagen I to facilitate the generation of large COPII carriers. Proceedings of the National Academy of Sciences of the United States of America 42 30545919
2020 It takes more than two to tango: mechanosignaling of the endothelial surface. Pflugers Archiv : European journal of physiology 41 32239285
2008 The bovine papillomavirus E5 protein and the PDGF beta receptor: it takes two to tango. Virology 41 18990418
2019 It takes two (centrioles) to tango. Reproduction (Cambridge, England) 40 30496124
2008 Immunogenicity of DNA vaccines in humans: it takes two to tango. Human vaccines 40 18443427
2019 Tango1 coordinates the formation of endoplasmic reticulum/Golgi docking sites to mediate secretory granule formation. The Journal of biological chemistry 39 31690624
2012 The KCNE Tango - How KCNE1 Interacts with Kv7.1. Frontiers in pharmacology 39 22876232
2021 Exosomal miR-30a and miR-222 derived from colon cancer mesenchymal stem cells promote the tumorigenicity of colon cancer through targeting MIA3. Journal of gastrointestinal oncology 37 33708424
2013 It takes two to tango--signalling by dimeric Raf kinases. Molecular bioSystems 36 23212737
2006 TANGO is a tumor suppressor of malignant melanoma. International journal of cancer 35 17044017
2020 A physical mechanism of TANGO1-mediated bulky cargo export. eLife 34 33169667
2012 Protein tango: the toolbox to capture interacting partners. Angewandte Chemie (International ed. in English) 34 22689479
2008 Specificity of signaling from MAPKs to MAPKAPKs: kinases' tango nuevo. Frontiers in bioscience : a journal and virtual library 33 18508642
2004 Characterization and expression pattern of the novel MIA homolog TANGO. Gene expression patterns : GEP 33 15183315
2020 Two to Tango: Dialogue between Adaptive and Innate Immunity in Type 1 Diabetes. Journal of diabetes research 32 32802890
2009 Utilization of the Tango beta-arrestin recruitment technology for cell-based EDG receptor assay development and interrogation. Journal of biomolecular screening 32 19726785
2003 It takes two to tango: mast cell and Schwann cell interactions in neurofibromas. The Journal of clinical investigation 32 14679174
2022 It Takes More than Two to Tango: Complex, Hierarchal, and Membrane-Modulated Interactions in the Regulation of Receptor Tyrosine Kinases. Cancers 31 35205690
2021 YAP/Hippo Pathway and Cancer Immunity: It Takes Two to Tango. Biomedicines 31 34944765
2021 A general role for TANGO1, encoded by MIA3, in secretory pathway organization and function. Journal of cell science 29 34350936
2020 TANGO1 membrane helices create a lipid diffusion barrier at curved membranes. eLife 29 32452385
2017 Identification of a molecular signaling gene-gene regulatory network between GWAS susceptibility genes ADTRP and MIA3/TANGO1 for coronary artery disease. Biochimica et biophysica acta. Molecular basis of disease 29 28341552
2017 WNT Takes Two to Tango: Molecular Links between the Circadian Clock and the Cell Cycle in Adult Stem Cells. Journal of biological rhythms 29 29277155
2021 Loss of TANGO1 Leads to Absence of Bone Mineralization. JBMR plus 28 33778321
2021 TANGO1 marshals the early secretory pathway for cargo export. Biochimica et biophysica acta. Biomembranes 28 34293283
2020 It takes two to tango - molecular links between plant immunity and brassinosteroid signalling. Journal of cell science 28 33239345
2007 Reduced expression of TANGO in colon and hepatocellular carcinomas. Oncology reports 28 17786351
2002 The GoLoco motif: heralding a new tango between G protein signaling and cell division. Molecular interventions 28 14993354
2022 A tango for coats and membranes: New insights into ER-to-Golgi traffic. Cell reports 27 35045300
2020 Complex Interplay between the RUNX Transcription Factors and Wnt/β-Catenin Pathway in Cancer: A Tango in the Night. Molecules and cells 27 32041394
2014 Diagnostics and treatment of cryoglobulinaemia: it takes two to tango. Clinical reviews in allergy & immunology 27 24068540
2022 Immunomodulation by foods and microbes: Unravelling the molecular tango. Allergy 26 35892227
2017 TANGO - a screening tool to identify comorbidities on the causal pathway of nocturia. BJU international 26 28075514
2020 Mitotic ER Exit Site Disassembly and Reassembly Are Regulated by the Phosphorylation Status of TANGO1. Developmental cell 25 32818468
2013 It takes two to tango: Ubiquitin and SUMO in the DNA damage response. Frontiers in genetics 25 23781231
2021 Macrophages and Stem Cells-Two to Tango for Tissue Repair? Biomolecules 24 34066618
2017 MicroRNA-222 influences migration and invasion through MIA3 in colorectal cancer. Cancer cell international 24 28855850
2023 The Tango between Cancer-Associated Fibroblasts (CAFs) and Immune Cells in Affecting Immunotherapy Efficacy in Pancreatic Cancer. International journal of molecular sciences 23 37240052
2009 Kappa opioid receptor screen with the Tango beta-arrestin recruitment technology and characterization of hits with second-messenger assays. Journal of biomolecular screening 23 19403921
2020 It takes two to tango: coupling of Hippo pathway and redox signaling in biological process. Cell cycle (Georgetown, Tex.) 22 33016196
2013 Meta-analysis identifies robust association between SNP rs17465637 in MIA3 on chromosome 1q41 and coronary artery disease. Atherosclerosis 22 24125424
2012 Two to tango: GPCR oligomers and GPCR-TRP channel interactions in nociception. Life sciences 22 22771696
2009 It takes two to tango: combinations of conventional cytotoxics with compounds targeting the vascular endothelial growth factor-vascular endothelial growth factor receptor pathway in patients with solid malignancies. Cancer science 22 19860846
2023 Redox sensitive human mitochondrial aconitase and its interaction with frataxin: In vitro and in silico studies confirm that it takes two to tango. Free radical biology & medicine 21 36738801
2022 Synergistic hydroxyl radical formation, system XC- inhibition and heat shock protein crosslinking tango in ferrotherapy: A prove-of-concept study of "sword and shield" theory. Materials today. Bio 21 35865409
2007 Interactions of TANGO and leukocyte integrin CD11c/CD18 regulate the migration of human monocytes. Journal of leukocyte biology 21 17726152
2005 Analysis of the transcriptional activation domain of the Drosophila tango bHLH-PAS transcription factor. Development genes and evolution 21 15818484

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