Milošević, Ira

[["dc.bibliographiccitation.firstpage","232"],["dc.bibliographiccitation.issue","2"],["dc.bibliographiccitation.journal","EMBO reports"],["dc.bibliographiccitation.lastpage","9"],["dc.bibliographiccitation.volume","16"],["dc.contributor.author","Pechstein, Arndt"],["dc.contributor.author","Gerth, Fabian"],["dc.contributor.author","Milosevic, Ira"],["dc.contributor.author","Jäpel, Maria"],["dc.contributor.author","Eichhorn-Grünig, Marielle"],["dc.contributor.author","Vorontsova, Olga"],["dc.contributor.author","Bacetic, Jelena"],["dc.contributor.author","Maritzen, Tanja"],["dc.contributor.author","Shupliakov, Oleg"],["dc.contributor.author","Freund, Christian"],["dc.contributor.author","Haucke, Volker"],["dc.date.accessioned","2019-07-09T11:41:09Z"],["dc.date.available","2019-07-09T11:41:09Z"],["dc.date.issued","2015-02-01"],["dc.description.abstract","Neurotransmission involves the exo-endocytic cycling of synaptic vesicle (SV) membranes. Endocytic membrane retrieval and clathrin-mediated SV reformation require curvature-sensing and membrane-bending BAR domain proteins such as endophilin A. While their ability to sense and stabilize curved membranes facilitates membrane recruitment of BAR domain proteins, the precise mechanisms by which they are targeted to specific sites of SV recycling has remained unclear. Here, we demonstrate that the multi-domain scaffold intersectin 1 directly associates with endophilin A to facilitate vesicle uncoating at synapses. Knockout mice deficient in intersectin 1 accumulate clathrin-coated vesicles at synapses, a phenotype akin to loss of endophilin function. Intersectin 1/endophilin A1 complex formation is mediated by direct binding of the SH3B domain of intersectin to a non-canonical site on the SH3 domain of endophilin A1. Consistent with this, intersectin-binding defective mutant endophilin A1 fails to rescue clathrin accumulation at neuronal synapses derived from endophilin A1-3 triple knockout (TKO) mice. Our data support a model in which intersectin aids endophilin A recruitment to sites of clathrin-mediated SV recycling, thereby facilitating vesicle uncoating."],["dc.identifier.doi","10.15252/embr.201439260"],["dc.identifier.fs","610968"],["dc.identifier.pmid","25520322"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/11737"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/58362"],["dc.language.iso","en"],["dc.notes.intern","Merged from goescholar"],["dc.relation","info:eu-repo/grantAgreement/EC/FP7/242167/EU//SYNSYS"],["dc.relation.euproject","SynSys"],["dc.relation.issn","1469-3178"],["dc.rights","CC BY 4.0"],["dc.rights.uri","https://creativecommons.org/licenses/by/4.0"],["dc.title","Vesicle uncoating regulated by SH3-SH3 domain-mediated complex formation between endophilin and intersectin at synapses."],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","10a"],["dc.bibliographiccitation.issue","3"],["dc.bibliographiccitation.journal","Biophysical Journal"],["dc.bibliographiccitation.volume","116"],["dc.contributor.author","Milosevic, Ira"],["dc.date.accessioned","2020-12-10T14:22:45Z"],["dc.date.available","2020-12-10T14:22:45Z"],["dc.date.issued","2019"],["dc.identifier.doi","10.1016/j.bpj.2018.11.091"],["dc.identifier.issn","0006-3495"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/71721"],["dc.language.iso","en"],["dc.notes.intern","DOI Import GROB-354"],["dc.title","Regulation of Vesicle Acidification at the Neuronal Synapse"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","jcs236737"],["dc.bibliographiccitation.issue","2"],["dc.bibliographiccitation.journal","Journal of Cell Science"],["dc.bibliographiccitation.volume","133"],["dc.contributor.author","Kroll, Jana"],["dc.contributor.author","Özçete, Özge Demet"],["dc.contributor.author","Jung, Sangyong"],["dc.contributor.author","Maritzen, Tanja"],["dc.contributor.author","Milosevic, Ira"],["dc.contributor.author","Wichmann, Carolin"],["dc.contributor.author","Moser, Tobias"],["dc.date.accessioned","2020-12-10T18:41:54Z"],["dc.date.available","2020-12-10T18:41:54Z"],["dc.date.issued","2020"],["dc.identifier.doi","10.1242/jcs.236737"],["dc.identifier.eissn","1477-9137"],["dc.identifier.issn","0021-9533"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/77721"],["dc.language.iso","en"],["dc.notes.intern","DOI Import GROB-354"],["dc.title","AP180 promotes release site clearance and clathrin-dependent vesicle reformation in mouse cochlear inner hair cells"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","2407"],["dc.bibliographiccitation.issue","9"],["dc.bibliographiccitation.journal","Aging"],["dc.bibliographiccitation.lastpage","2427"],["dc.bibliographiccitation.volume","10"],["dc.contributor.author","Musa, Marina"],["dc.contributor.author","Perić, Matea"],["dc.contributor.author","Bou Dib, Peter"],["dc.contributor.author","Sobočanec, Sandra"],["dc.contributor.author","Šarić, Ana"],["dc.contributor.author","Lovrić, Anita"],["dc.contributor.author","Rudan, Marina"],["dc.contributor.author","Nikolić, Andrea"],["dc.contributor.author","Milosević, Ira"],["dc.contributor.author","Vlahoviček, Kristian"],["dc.contributor.author","Raimundo, Nuno"],["dc.contributor.author","Kriško, Anita"],["dc.date.accessioned","2020-12-10T18:42:49Z"],["dc.date.available","2020-12-10T18:42:49Z"],["dc.date.issued","2018"],["dc.identifier.doi","10.18632/aging.v10i9"],["dc.identifier.eissn","1945-4589"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/78101"],["dc.language.iso","en"],["dc.notes.intern","DOI Import GROB-354"],["dc.title","Heat-induced longevity in budding yeast requires respiratory metabolism and glutathione recycling"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.artnumber","27"],["dc.bibliographiccitation.journal","Frontiers in Cellular Neuroscience"],["dc.bibliographiccitation.volume","12"],["dc.contributor.author","Milosevic, Ira"],["dc.date.accessioned","2019-07-09T11:45:08Z"],["dc.date.available","2019-07-09T11:45:08Z"],["dc.date.issued","2018"],["dc.description.abstract","Without robust mechanisms to efficiently form new synaptic vesicles (SVs), the tens to hundreds of SVs typically present at the neuronal synapse would be rapidly used up, even at modest levels of neuronal activity. SV recycling is thus critical for synaptic physiology and proper function of sensory and nervous systems. Yet, more than four decades after it was originally proposed that the SVs are formed and recycled locally at the presynaptic terminals, the mechanisms of endocytic processes at the synapse are heavily debated. Clathrin-mediated endocytosis, a type of endocytosis that capitalizes on the clathrin coat, a number of adaptor and accessory proteins, and the GTPase dynamin, is well understood, while the contributions of clathrin-independent fast endocytosis, kiss-and-run, bulk endocytosis and ultrafast endocytosis are still being evaluated. This review article revisits and summarizes the current knowledge on the SV reformation with a focus on clathrin-mediated endocytosis, and it discusses the modes of SV formation from endosome-like structures at the synapse. Given the importance of this topic, future advances in this active field are expected to contribute to better comprehension of neurotransmission, and to have general implications for neuroscience and medicine."],["dc.identifier.doi","10.3389/fncel.2018.00027"],["dc.identifier.pmid","29467622"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/15037"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/59162"],["dc.language.iso","en"],["dc.notes.intern","Merged from goescholar"],["dc.relation.issn","1662-5102"],["dc.rights","CC BY 4.0"],["dc.rights.uri","https://creativecommons.org/licenses/by/4.0"],["dc.subject.ddc","610"],["dc.title","Revisiting the Role of Clathrin-Mediated Endoytosis in Synaptic Vesicle Recycling"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","1184"],["dc.bibliographiccitation.issue","6"],["dc.bibliographiccitation.journal","Neuron"],["dc.bibliographiccitation.lastpage","1197.e6"],["dc.bibliographiccitation.volume","98"],["dc.contributor.author","Watanabe, Shigeki"],["dc.contributor.author","Mamer, Lauren Elizabeth"],["dc.contributor.author","Raychaudhuri, Sumana"],["dc.contributor.author","Luvsanjav, Delgermaa"],["dc.contributor.author","Eisen, Julia"],["dc.contributor.author","Trimbuch, Thorsten"],["dc.contributor.author","Söhl-Kielczynski, Berit"],["dc.contributor.author","Fenske, Pascal"],["dc.contributor.author","Milosevic, Ira"],["dc.contributor.author","Rosenmund, Christian"],["dc.contributor.author","Jorgensen, Erik M."],["dc.date.accessioned","2020-12-10T15:20:29Z"],["dc.date.available","2020-12-10T15:20:29Z"],["dc.date.issued","2018"],["dc.identifier.doi","10.1016/j.neuron.2018.06.005"],["dc.identifier.issn","0896-6273"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/72685"],["dc.language.iso","en"],["dc.notes.intern","DOI Import GROB-354"],["dc.title","Synaptojanin and Endophilin Mediate Neck Formation during Ultrafast Endocytosis"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.issue","1"],["dc.bibliographiccitation.journal","Nature Communications"],["dc.bibliographiccitation.volume","11"],["dc.contributor.author","Sathyanarayanan, Udhayabhaskar"],["dc.contributor.author","Musa, Marina"],["dc.contributor.author","Bou Dib, Peter"],["dc.contributor.author","Raimundo, Nuno"],["dc.contributor.author","Milosevic, Ira"],["dc.contributor.author","Krisko, Anita"],["dc.date.accessioned","2021-04-14T08:31:49Z"],["dc.date.available","2021-04-14T08:31:49Z"],["dc.date.issued","2020"],["dc.description.sponsorship","Open-Access-Publikationsfonds 2021"],["dc.identifier.doi","10.1038/s41467-020-19104-1"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/83720"],["dc.language.iso","en"],["dc.notes.intern","DOI Import GROB-399"],["dc.relation.eissn","2041-1723"],["dc.relation.orgunit","Abteilung Experimentelle Neurodegeneration"],["dc.rights","CC BY 4.0"],["dc.title","ATP hydrolysis by yeast Hsp104 determines protein aggregate dissolution and size in vivo"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.subtype","original_ja"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.artnumber","45076"],["dc.bibliographiccitation.journal","Scientific Reports"],["dc.bibliographiccitation.volume","7"],["dc.contributor.author","Fernandez-Mosquera, Lorena"],["dc.contributor.author","Diogo, Catia V."],["dc.contributor.author","Yambire, King Faisal"],["dc.contributor.author","Santos, Gabriela L."],["dc.contributor.author","Luna Sanchez, Marta"],["dc.contributor.author","Benit, Paule"],["dc.contributor.author","Rustin, Pierre"],["dc.contributor.author","Carlos Lopez, Luis"],["dc.contributor.author","Milosevic, Ira"],["dc.contributor.author","Raimundo, Nuno"],["dc.date.accessioned","2018-11-07T10:26:02Z"],["dc.date.available","2018-11-07T10:26:02Z"],["dc.date.issued","2017"],["dc.description.abstract","Mitochondria are key cellular signaling platforms, affecting fundamental processes such as cell proliferation, differentiation and death. However, it remains unclear how mitochondrial signaling affects other organelles, particularly lysosomes. Here, we demonstrate that mitochondrial respiratory chain (RC) impairments elicit a stress signaling pathway that regulates lysosomal biogenesis via the microphtalmia transcription factor family. Interestingly, the effect of mitochondrial stress over lysosomal biogenesis depends on the timeframe of the stress elicited: while RC inhibition with rotenone or uncoupling with CCCP initially triggers lysosomal biogenesis, the effect peaks after few hours and returns to baseline. Long-term RC inhibition by long-term treatment with rotenone, or patient mutations in fibroblasts and in a mouse model result in repression of lysosomal biogenesis. The induction of lysosomal biogenesis by short-term mitochondrial stress is dependent on TFEB and MITF, requires AMPK signaling and is independent of calcineurin signaling. These results reveal an integrated view of how mitochondrial signaling affects lysosomes, which is essential to fully comprehend the consequences of mitochondrial malfunction, particularly in the context of mitochondrial diseases."],["dc.description.sponsorship","Open-Access-Publikationsfonds 2017"],["dc.identifier.doi","10.1038/srep45076"],["dc.identifier.isi","000397760800001"],["dc.identifier.pmid","28345620"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/14396"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/42963"],["dc.notes.intern","Merged from goescholar"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","PUB_WoS_Import"],["dc.publisher","Nature Publishing Group"],["dc.relation.issn","2045-2322"],["dc.rights","CC BY 4.0"],["dc.rights.uri","https://creativecommons.org/licenses/by/4.0"],["dc.title","Acute and chronic mitochondrial respiratory chain deficiency differentially regulate lysosomal biogenesis"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.journal","eLife"],["dc.bibliographiccitation.volume","8"],["dc.contributor.author","Yambire, King Faisal"],["dc.contributor.author","Rostosky, Christine"],["dc.contributor.author","Watanabe, Takashi"],["dc.contributor.author","Pacheu-Grau, David"],["dc.contributor.author","Torres-Odio, Sylvia"],["dc.contributor.author","Sanchez-Guerrero, Angela"],["dc.contributor.author","Senderovich, Ola"],["dc.contributor.author","Meyron-Holtz, Esther G"],["dc.contributor.author","Milosevic, Ira"],["dc.contributor.author","Frahm, Jens"],["dc.contributor.author","West, A Phillip"],["dc.contributor.author","Raimundo, Nuno"],["dc.date.accessioned","2020-12-10T18:48:09Z"],["dc.date.available","2020-12-10T18:48:09Z"],["dc.date.issued","2019"],["dc.identifier.doi","10.7554/eLife.51031"],["dc.identifier.pmid","31793879"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/17114"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/79035"],["dc.identifier.url","https://sfb1190.med.uni-goettingen.de/production/literature/publications/104"],["dc.language.iso","en"],["dc.notes.intern","DOI Import GROB-354"],["dc.notes.intern","Merged from goescholar"],["dc.relation","SFB 1190: Transportmaschinen und Kontaktstellen zellulärer Kompartimente"],["dc.relation","SFB 1190 | P02: Charakterisierung der ER-Mitochondrien-Kontakte und ihre Rolle in der Signalweiterleitung"],["dc.relation.workinggroup","RG Milosevic (Synaptic Vesicle Dynamics)"],["dc.relation.workinggroup","RG Raimundo"],["dc.rights","CC BY 4.0"],["dc.rights.uri","https://creativecommons.org/licenses/by/4.0"],["dc.title","Impaired lysosomal acidification triggers iron deficiency and inflammation in vivo"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.subtype","original_ja"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","147"],["dc.bibliographiccitation.lastpage","160"],["dc.contributor.author","Milošević, Ira"],["dc.contributor.editor","Swan, Laura E."],["dc.date.accessioned","2022-08-26T07:50:14Z"],["dc.date.available","2022-08-26T07:50:14Z"],["dc.date.issued","2018"],["dc.description.abstract","Endocytosis is a well-orchestrated cascade of lipid-protein and protein-protein interactions resulting in formation and internalization of vesicles. Membrane phospholipids have key regulatory functions in endocytosis and membrane traffic. I have previously described an in vitro assay based on the isolated, substrate-attached plasma membrane to study the spatial distribution and levels of phosphoinositides, in particular phosphatidylinositol-4,5-bisphospate [PI(4,5)P2]. This assay utilizes cultured cells subjected to a brief ultrasonic pulse, resulting in the formation of thin, flat inside-out plasma membrane sheets with elements of cell cytoskeleton. Here, I describe an experimental procedure for \"on-stage\" and \"off-stage\" detection of PI(4,5)P2 spatial distribution, and semi-quantification of PI(4,5)P2 levels in the plasma membrane using fluorescence microscopy. Depending on the probe selected for lipid detection, this simple assay can be modified to study other plasmalemmal phospholipids and/or proteins."],["dc.identifier.doi","10.1007/978-1-4939-8719-1_11"],["dc.identifier.pmid","30129015"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/113250"],["dc.identifier.url","https://sfb1190.med.uni-goettingen.de/production/literature/publications/37"],["dc.language.iso","en"],["dc.publisher","Springer"],["dc.relation","SFB 1190: Transportmaschinen und Kontaktstellen zellulärer Kompartimente"],["dc.relation","SFB 1190 | P02: Charakterisierung der ER-Mitochondrien-Kontakte und ihre Rolle in der Signalweiterleitung"],["dc.relation.isbn","978-1-4939-8717-7"],["dc.relation.isbn","978-1-4939-8719-1"],["dc.relation.ispartof","Clathrin-Mediated Endocytosis. Methods and Protocols"],["dc.relation.workinggroup","RG Milosevic (Synaptic Vesicle Dynamics)"],["dc.title","Spatial and Temporal Aspects of Phosphoinositides in Endocytosis Studied in the Isolated Plasma Membranes"],["dc.type","book_chapter"],["dc.type.internalPublication","unknown"],["dspace.entity.type","Publication"]]