2025
BPS2025 - A role for the bridge-like lipid transfer protein VPS13D in the control of membrane dynamics at the trans Golgi/TGN
Amos C, Fujise K, Ugur B, Hanna M, Xu P, De Camilli P. BPS2025 - A role for the bridge-like lipid transfer protein VPS13D in the control of membrane dynamics at the trans Golgi/TGN. Biophysical Journal 2025, 124: 274a-275a. DOI: 10.1016/j.bpj.2024.11.1556.Peer-Reviewed Original ResearchBPS2025 - A role for the bridge-like lipid transfer protein VPS13D in the control of membrane dynamics at the trans Golgi/TGN
Amos C, Fujise K, Ugur B, Hanna M, Xu P, De Camilli P. BPS2025 - A role for the bridge-like lipid transfer protein VPS13D in the control of membrane dynamics at the trans Golgi/TGN. Biophysical Journal 2025, 124: 358a. DOI: 10.1016/j.bpj.2024.11.1947.Peer-Reviewed Original Research
2024
VPS13B is localized at the interface between Golgi cisternae and is a functional partner of FAM177A1
Ugur B, Schueder F, Shin J, Hanna M, Wu Y, Leonzino M, Su M, McAdow A, Wilson C, Postlethwait J, Solnica-Krezel L, Bewersdorf J, De Camilli P. VPS13B is localized at the interface between Golgi cisternae and is a functional partner of FAM177A1. Journal Of Cell Biology 2024, 223: e202311189. PMID: 39331042, PMCID: PMC11451052, DOI: 10.1083/jcb.202311189.Peer-Reviewed Original ResearchConceptsLipid transportGolgi complex proteinGolgi subcompartmentsGolgi membranesGolgi cisternaeProtein familyFunctional partnersGolgi complexKO cellsComplex proteinsFAM177A1GolgiVPS13BAdjacent membranesMutationsProteinCohen syndromeLipidOrthologsInteractorsBrefeldinMembraneOrganellesSubcompartmentsDevelopmental disordersLoss of function of FAM177A1, a Golgi complex localized protein, causes a novel neurodevelopmental disorder
Kohler J, Legro N, Baldridge D, Shin J, Bowman A, Ugur B, Jackstadt M, Shriver L, Patti G, Zhang B, Feng W, McAdow A, Goddard P, Ungar R, Jensen T, Smith K, Fresard L, Alvarez R, Bonner D, Reuter C, McCormack C, Kravets E, Marwaha S, Holt J, Network U, Acosta M, Adam M, Adams D, Alvarez R, Alvey J, Amendola L, Andrews A, Ashley E, Bacino C, Bademci G, Balasubramanyam A, Baldridge D, Bale J, Bamshad M, Barbouth D, Bayrak-Toydemir P, Beck A, Beggs A, Behrens E, Bejerano G, Bellen H, Bennett J, Berg-Rood B, Bernstein J, Berry G, Bican A, Bivona S, Blue E, Bohnsack J, Bonner D, Botto L, Boyd B, Briere L, Burke E, Burrage L, Butte M, Byers P, Byrd W, Carey J, Carrasquillo O, Cassini T, Chang T, Chanprasert S, Chao H, Chinn I, Clark G, Coakley T, Cobban L, Cogan J, Coggins M, Cole F, Colley H, Cope H, Corner B, Corona R, Craigen W, Crouse A, Cunningham M, D’Souza P, Dai H, Dasari S, Davis J, Dayal J, Dell’Angelica E, Dickson P, Dipple K, Doherty D, Dorrani N, Doss A, Douine E, Earl D, Eckstein D, Emrick L, Eng C, Ezell K, Falk M, Fieg E, Fisher P, Fogel B, Forghani I, Gahl W, Glass I, Gochuico B, Goddard P, Godfrey R, Golden-Grant K, Grajewski A, Hadley D, Hahn S, Halley M, Hamid R, Hassey K, Hayes N, High F, Hing A, Hisama F, Holm I, Hom J, Horike-Pyne M, Huang A, Hutchison S, Introne W, Isasi R, Izumi K, Jamal F, Jarvik G, Jarvik J, Jayadev S, Jean-Marie O, Jobanputra V, Karaviti L, Ketkar S, Kiley D, Kilich G, Kobren S, Kohane I, Kohler J, Korrick S, Kozuira M, Krakow D, Krasnewich D, Kravets E, Lalani S, Lam B, Lam C, Lanpher B, Lanza I, LeBlanc K, Lee B, Levitt R, Lewis R, Liu P, Liu X, Longo N, Loo S, Loscalzo J, Maas R, Macnamara E, MacRae C, Maduro V, Maghiro A, Mahoney R, Malicdan M, Mamounas L, Manolio T, Mao R, Maravilla K, Marom R, Marth G, Martin B, Martin M, MartÃnez-Agosto J, Marwaha S, McCauley J, McConkie-Rosell A, McCray A, McGee E, Mefford H, Merritt J, Might M, Mirzaa G, Morava E, Moretti P, Mulvihill J, Nakano-Okuno M, Nelson S, Neumann S, Newman J, Nicholas S, Nickerson D, Nieves-Rodriguez S, Novacic D, Oglesbee D, Orengo J, Pace L, Pak S, Pallais J, Palmer C, Papp J, Parker N, Phillips J, Posey J, Potocki L, Swerdzewski B, Quinlan A, Rao D, Raper A, Raskind W, Renteria G, Reuter C, Rives L, Robertson A, Rodan L, Rosenfeld J, Rosenwasser N, Rossignol F, Ruzhnikov M, Sacco R, Sampson J, Saporta M, Schaechter J, Schedl T, Schoch K, Scott D, Scott C, Seto E, Shashi V, Shin J, Silverman E, Sinsheimer J, Sisco K, Smith E, Smith K, Solnica-Krezel L, Solomon B, Spillmann R, Stoler J, Sullivan K, Sullivan J, Sun A, Sutton S, Sweetser D, Sybert V, Tabor H, Tan Q, Tan A, Tarakad A, Tekin M, Telischi F, Thorson W, Tifft C, Toro C, Tran A, Ungar R, Urv T, Vanderver A, Velinder M, Viskochil D, Vogel T, Wahl C, Walker M, Wallace S, Walley N, Wambach J, Wan J, Wangler M, Ward P, Wegner D, Hubshman M, Wener M, Wenger T, Westerfield M, Wheeler M, Whitlock J, Wolfe L, Worley K, Xiao C, Yamamoto S, Yang J, Zhang Z, Zuchner S, Worthey E, Ashley E, Montgomery S, Fisher P, Postlethwait J, De Camilli P, Solnica-Krezel L, Bernstein J, Wheeler M. Loss of function of FAM177A1, a Golgi complex localized protein, causes a novel neurodevelopmental disorder. Genetics In Medicine 2024, 26: 101166. PMID: 38767059, PMCID: PMC11451386, DOI: 10.1016/j.gim.2024.101166.Peer-Reviewed Original ResearchNegative regulation of cell proliferationLoss-of-function variantsPathways associated with apoptosisRegulation of cell proliferationRelationship to human diseaseHuman cell linesNeurodevelopmental disordersRNA-seqLocalized proteinsImmune-associated genesZebrafish cellsGolgi complexModel organismsGlobal developmental delayBiallelic variantsFAM177A1Negative regulatorHuman diseasesZebrafish model organismPhysiological functionsCell linesGolgiHuman fibroblastsZebrafishCell proliferation
2022
A partnership between the lipid scramblase XK and the lipid transfer protein VPS13A at the plasma membrane
Guillén-Samander A, Wu Y, Pineda SS, GarcÃa FJ, Eisen JN, Leonzino M, Ugur B, Kellis M, Heiman M, De Camilli P. A partnership between the lipid scramblase XK and the lipid transfer protein VPS13A at the plasma membrane. Proceedings Of The National Academy Of Sciences Of The United States Of America 2022, 119: e2205425119. PMID: 35994651, PMCID: PMC9436381, DOI: 10.1073/pnas.2205425119.Peer-Reviewed Original ResearchConceptsCaudate neuronsClinical manifestationsExposure of PtdSerPH domainMcLeod syndromeCell surface exposureER-PM contactsLipid dropletsTransport of lipidsPutative roleUnknown mechanismNeuronsLipid transfer proteinVPS13ALipid scramblasesTransfer proteinCytosolic loopExposurePlasma membraneCell surfaceEndoplasmic reticulumLipid transferERSyndromeDisease
2020
Role of VPS13, a protein with similarity to ATG2, in physiology and disease
Ugur B, Hancock-Cerutti W, Leonzino M, De Camilli P. Role of VPS13, a protein with similarity to ATG2, in physiology and disease. Current Opinion In Genetics & Development 2020, 65: 61-68. PMID: 32563856, PMCID: PMC7746581, DOI: 10.1016/j.gde.2020.05.027.Peer-Reviewed Original ResearchConceptsAutophagy protein ATG2N-terminal halfVPS13 proteinsMolecular functionsCellular processesFamily proteinsVps13Contact sitesAtg2Intracellular organellesFunctional studiesNovel mechanismProteinSimilar roleHydrophobic channelStructural studiesNeurodegenerative disordersPhysiologyDirect transferOrganellesSimilarityMutationsRoleLipidsBilayers
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