2024
Endoplasmic reticulum exit sites are segregated for secretion based on cargo size
Saxena S, Foresti O, Liu A, Androulaki S, Pena Rodriguez M, Raote I, Aridor M, Cui B, Malhotra V. Endoplasmic reticulum exit sites are segregated for secretion based on cargo size. Developmental Cell 2024, 59: 2593-2608.e6. PMID: 38991587, PMCID: PMC11813558, DOI: 10.1016/j.devcel.2024.06.009.Peer-Reviewed Original ResearchEndoplasmic reticulum exit sitesProline-rich domainC-terminal proline-rich domainCOPII assemblyExit siteER membraneCargo exportJuxtanuclear regionU2OS cellsCargo moleculesBulky cargoSEC23AOptimal secretionCollagen VIIHuman osteosarcomaProlonged bindingComplex organismsCargoCargo sizeBindingCollagen ICTAGE5TANGO1COPIIERGIC53TANGO1 inhibitors reduce collagen secretion and limit tissue scarring
Raote I, Rosendahl A, Häkkinen H, Vibe C, Küçükaylak I, Sawant M, Keufgens L, Frommelt P, Halwas K, Broadbent K, Cunquero M, Castro G, Villemeur M, Nüchel J, Bornikoel A, Dam B, Zirmire R, Kiran R, Carolis C, Andilla J, Loza-Alvarez P, Ruprecht V, Jamora C, Campelo F, Krüger M, Hammerschmidt M, Eckes B, Neundorf I, Krieg T, Malhotra V. TANGO1 inhibitors reduce collagen secretion and limit tissue scarring. Nature Communications 2024, 15: 3302. PMID: 38658535, PMCID: PMC11043333, DOI: 10.1038/s41467-024-47004-1.Peer-Reviewed Original ResearchConceptsEndoplasmic reticulum exit sitesECM proteinsSecretion of ECM proteinsPeptide inhibitorFibrotic diseasesCollagen exportTANGO1Binding interfaceWound healingZebrafish resultsECM componentsReduced granulation tissue formationGranulation tissue formationEffective therapyCutaneous wound healingInhibitor treatmentFibrotic processUncontrolled secretionWidespread occurrenceProtein levelsExit siteExcessive scarringAmount of collagenTherapeutic modulationTissue scarringCOPII with ALG2 and ESCRTs control lysosome-dependent microautophagy of ER exit sites
Liao Y, Pang S, Li W, Shtengel G, Choi H, Schaefer K, Xu C, Lippincott-Schwartz J. COPII with ALG2 and ESCRTs control lysosome-dependent microautophagy of ER exit sites. Developmental Cell 2024, 59: 1410-1424.e4. PMID: 38593803, DOI: 10.1016/j.devcel.2024.03.027.Peer-Reviewed Original ResearchEndoplasmic reticulum exit sitesER exit sitesAmino acid starvationPurified recombinant componentsExit siteProtein sortingSecretory pathwayMammalian cellsNutrient stressCellular conditionsEndoplasmic reticulumGiant unilamellar vesiclesTubular outgrowthsESCRTMicroautophagyNutrient stressorsALG2COPIILysosomesPathwayMTOR inhibitionUnilamellar vesiclesRecombinant componentsFocused Ion Beam Scanning Electron MicroscopyIon beam scanning electron microscopy
2011
The Ubiquitin Regulatory X (UBX) Domain-containing Protein TUG Regulates the p97 ATPase and Resides at the Endoplasmic Reticulum-Golgi Intermediate Compartment*
Orme CM, Bogan JS. The Ubiquitin Regulatory X (UBX) Domain-containing Protein TUG Regulates the p97 ATPase and Resides at the Endoplasmic Reticulum-Golgi Intermediate Compartment*. Journal Of Biological Chemistry 2011, 287: 6679-6692. PMID: 22207755, PMCID: PMC3307297, DOI: 10.1074/jbc.m111.284232.Peer-Reviewed Original ResearchMeSH KeywordsAdenosine TriphosphatasesBiological TransportCell Cycle ProteinsEndoplasmic ReticulumGene ExpressionGene Knockdown TechniquesGolgi ApparatusHEK293 CellsHeLa CellsHumansIntracellular Signaling Peptides and ProteinsOncogene Proteins, FusionProtein Structure, QuaternaryProtein Structure, TertiaryProtein TransportUbiquitinValosin Containing ProteinConceptsUBX domainIntermediate compartmentEndoplasmic reticulum-Golgi intermediate compartmentEndoplasmic reticulum exit sitesEarly secretory pathwayGolgi intermediate compartmentATP-bound stateP97/VCPN-terminal domainN-terminal regionP97 hexamerUbiquitylated proteinsHexameric ATPaseUbiquitylated substratesP97 activityCellular processesSecretory pathwayOligomeric statusMembrane fusionC-terminusGolgi complexEndoplasmic reticulumHEK293 cellsCell typesHeLa cells
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