Adjunct Faculty
Adjunct faculty typically have an academic or research appointment at another institution and contribute or collaborate with one or more School of Medicine faculty members or programs.
Adjunct rank detailsVivek Malhotra
Professor AdjunctAbout
Research
Publications
2025
ER tubular body: an ER-derived compartment for redirecting autophagy to secretory functions
Song M, Sim H, Noh S, Malhotra V, Lee M. ER tubular body: an ER-derived compartment for redirecting autophagy to secretory functions. Autophagy 2025, 21: 2082-2084. PMID: 40390263, PMCID: PMC12363525, DOI: 10.1080/15548627.2025.2508935.Peer-Reviewed Original ResearchPositive-strand RNA virusesConditions of cellular stressFormation of membrane compartmentsER-derived compartmentSecretion of proteinsCell surface traffickingReticulophagy receptorER remodelingVesicle traffickingProtein homeostasisMembrane compartmentsEndoplasmic reticulumActivation of UCPRNA virusesTransmembrane proteinsCellular stressProtein secretionTrafficking defectTubulovesicular networkPotential therapeutic strategyViral pathogenesisProteinViral replicationSecretory functionTubular bodyThe pathways of secretory cargo export at the endoplasmic reticulum
Malhotra V. The pathways of secretory cargo export at the endoplasmic reticulum. Nature Communications 2025, 16: 2138. PMID: 40032897, PMCID: PMC11876584, DOI: 10.1038/s41467-025-57408-2.Peer-Reviewed Original ResearchTANGO2 is an acyl-CoA binding protein
Lujan A, Foresti O, Wojnacki J, Bigliani G, Brouwers N, Pena M, Androulaki S, Hashidate-Yoshida T, Kalyukina M, Novoselov S, Shindou H, Malhotra V. TANGO2 is an acyl-CoA binding protein. Journal Of Cell Biology 2025, 224: e202410001. PMID: 40015245, PMCID: PMC11867700, DOI: 10.1083/jcb.202410001.Peer-Reviewed Original ResearchConceptsAcyl-CoA binding proteinPeriphery of lipid dropletsAcyl-coenzyme A binding proteinA-binding proteinsAcyl-coenzyme AMitochondrial lumenHeme transportBinding proteinTANGO2Cellular localizationLipid dropletsStructural regionsLipid metabolismHeightened energy demandsMutationsProteinResiduesNrdEMetabolic crisisBindingMetabolismHemeSevere cardiomyopathyLipidThe pathway of unconventional protein secretion involves CUPS and a modified trans-Golgi network
Curwin A, Kurokawa K, Bigliani G, Brouwers N, Nakano A, Malhotra V. The pathway of unconventional protein secretion involves CUPS and a modified trans-Golgi network. Journal Of Cell Biology 2025, 224: e202312120. PMID: 40015244, PMCID: PMC11867701, DOI: 10.1083/jcb.202312120.Peer-Reviewed Original ResearchConceptsTrans-Golgi networkUnconventional protein secretionUnconventional secretionSuper-resolution confocal live imaging microscopyProtein secretionPhosphatidylinositol 3-phosphatePhosphatidylinositol 4-phosphateExtracts of membranesGolgi membranesConventional secretionGolgi cisternaeMembrane fusionSecreted proteinsCup formationPI4PRCY1Drs2GolgiProteinPhosphatidylinositolSecretionMembraneCOPIIImaging microscopyBiogenesisDendritic cell phagosomes recruit GRASP55 for export of antigen-loaded MHC molecules
Cebrian I, Dinamarca S, Rodríguez M, Priego E, Brouwers N, Barends M, Brunnberg J, Tampé R, Blanchard N, Sancho D, Malhotra V. Dendritic cell phagosomes recruit GRASP55 for export of antigen-loaded MHC molecules. Cell Reports 2025, 44: 115333. PMID: 39955774, PMCID: PMC11861518, DOI: 10.1016/j.celrep.2025.115333.Peer-Reviewed Original ResearchConceptsExogenous antigen presentationDendritic cellsAntigen presentationMHC moleculesBone marrow-derived dendritic cellsBone marrow-derived DCCD4+ T cellsMHC-IActivated CD8+MHC class IIDendritic cell phagosomesMHC II moleculesCD8+Peptide-loaded MHC moleculesT cellsExogenous antigensMHC-IIClass IIAntigenEndocytic systemGRASP55Cell surfaceIntracellular transportPlasma membranePresentation
2024
524 Peptide inhibition of TANGO1 controls matrix accumulation in scarring and fibrosis
Rosendahl A, Raote I, Bornikoel A, Neundorf I, Hammerschmidt M, Krüger M, Malhotra V, Eckes B, Krieg T. 524 Peptide inhibition of TANGO1 controls matrix accumulation in scarring and fibrosis. Journal Of Investigative Dermatology 2024, 144: s319. DOI: 10.1016/j.jid.2024.10.537.Peer-Reviewed Original ResearchEndoplasmic 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 ICTAGE5TANGO1COPIIERGIC53Tailored assemblies of COPII proteins in secretion
Malhotra V. Tailored assemblies of COPII proteins in secretion. Journal Of Cell Biology 2024, 223: e202404013. PMID: 38958655, PMCID: PMC11222725, DOI: 10.1083/jcb.202404013.Peer-Reviewed Original ResearchTANGO1 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 scarringPublisher Correction: Pla2g12b drives expansion of triglyceride-rich lipoproteins
Thierer J, Foresti O, Yadav P, Wilson M, Moll T, Shen M, Busch-Nentwich E, Morash M, Mohlke K, Rawls J, Malhotra V, Hussain M, Farber S. Publisher Correction: Pla2g12b drives expansion of triglyceride-rich lipoproteins. Nature Communications 2024, 15: 2572. PMID: 38519494, PMCID: PMC10959976, DOI: 10.1038/s41467-024-46847-y.Peer-Reviewed Original Research