Fernández Busnadiego, Rubén

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[["dc.contributor.author","Saha, Itika"],["dc.contributor.author","Yuste-Checa, Patricia"],["dc.contributor.author","Silva Padilha, Miguel Da"],["dc.contributor.author","Guo, Qiang"],["dc.contributor.author","Körner, Roman"],["dc.contributor.author","Holthusen, Hauke"],["dc.contributor.author","Trinkaus, Victoria A."],["dc.contributor.author","Dudanova, Irina"],["dc.contributor.author","Fernández Busnadiego, Rubén"],["dc.contributor.author","Baumeister, Wolfgang"],["dc.contributor.author","Sanders, David W."],["dc.contributor.author","Gautam, Saurabh"],["dc.contributor.author","Diamond, Marc I."],["dc.contributor.author","Ulrich Hartl, F."],["dc.contributor.author","Hipp, Mark S."],["dc.date.accessioned","2022-04-06T12:10:37Z"],["dc.date.available","2022-04-06T12:10:37Z"],["dc.date.issued","2022"],["dc.identifier.doi","10.1101/2022.02.18.481043"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/106453"],["dc.identifier.url","https://mbexc.uni-goettingen.de/literature/publications/449"],["dc.relation","EXC 2067: Multiscale Bioimaging"],["dc.relation.workinggroup","RG Fernández-Busnadiego (Structural Cell Biology)"],["dc.title","The AAA+ chaperone VCP disaggregates Tau fibrils and generates aggregate seeds"],["dc.type","preprint"],["dc.type.internalPublication","yes"],["dspace.entity.type","Publication"]]

[["dc.contributor.author","Huang, Bin"],["dc.contributor.author","Guo, Qiang"],["dc.contributor.author","Niedermeier, Marie L."],["dc.contributor.author","Cheng, Jingdong"],["dc.contributor.author","Engler, Tatjana"],["dc.contributor.author","Maurer, Melanie"],["dc.contributor.author","Pautsch, Alexander"],["dc.contributor.author","Baumeister, Wolfgang"],["dc.contributor.author","Stengel, Florian"],["dc.contributor.author","Kochanek, Stefan"],["dc.contributor.author","Fernández Busnadiego, Rubén"],["dc.date.accessioned","2022-02-23T16:35:26Z"],["dc.date.available","2022-02-23T16:35:26Z"],["dc.date.issued","2021"],["dc.identifier.doi","10.1101/2021.02.02.429316"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/100375"],["dc.identifier.url","https://mbexc.uni-goettingen.de/literature/publications/231"],["dc.relation","EXC 2067: Multiscale Bioimaging"],["dc.relation.workinggroup","RG Fernández-Busnadiego (Structural Cell Biology)"],["dc.title","PolyQ expansion does not alter the Huntingtin-HAP40 complex"],["dc.type","preprint"],["dc.type.internalPublication","unknown"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","227"],["dc.bibliographiccitation.issue","3"],["dc.bibliographiccitation.journal","Journal of Huntington's Disease"],["dc.bibliographiccitation.lastpage","242"],["dc.bibliographiccitation.volume","11"],["dc.contributor.author","Seefelder, Manuel"],["dc.contributor.author","Klein, Fabrice A.C."],["dc.contributor.author","Landwehrmeyer, Bernhard"],["dc.contributor.author","Fernández-Busnadiego, Rubén"],["dc.contributor.author","Kochanek, Stefan"],["dc.date.accessioned","2022-09-01T09:51:05Z"],["dc.date.available","2022-09-01T09:51:05Z"],["dc.date.issued","2022"],["dc.description.abstract","Since the discovery of the mutation causing Huntington’s disease (HD) in 1993, it has been debated whether an expanded polyglutamine (polyQ) stretch affects the properties of the huntingtin (HTT) protein and thus contributes to the pathological mechanisms responsible for HD. Here we review the current knowledge about the structure of HTT, alone (apo-HTT) or in a complex with Huntingtin-Associated Protein 40 (HAP40), the influence of polyQ-length variation on apo-HTT and the HTT-HAP40 complex, and the biology of HAP40. Phylogenetic analyses suggest that HAP40 performs essential functions. Highlighting the relevance of its interaction with HTT, HAP40 is one of the most abundant partners copurifying with HTT and is rapidly degraded, when HTT levels are reduced. As the levels of both proteins decrease during disease progression, HAP40 could also be a biomarker for HD. Whether declining HAP40 levels contribute to disease etiology is an open question. Structural studies have shown that the conformation of apo-HTT is less constrained but resembles that adopted in the HTT-HAP40 complex, which is exceptionally stable because of extensive interactions between HAP40 and the three domains of HTT. The complex— and to some extent apo-HTT— resists fragmentation after limited proteolysis. Unresolved regions of apo-HTT, constituting about 25% of the protein, are the main sites of post-translational modifications and likely have major regulatory functions. PolyQ elongation does not substantially alter the structure of HTT, alone or when associated with HAP40. Particularly, polyQ above the disease length threshold does not induce drastic conformational changes in full-length HTT. Therefore, models of HD pathogenesis stating that polyQ expansion drastically alters HTT properties should be reconsidered."],["dc.identifier.doi","10.3233/JHD-220543"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/113880"],["dc.notes.intern","DOI-Import GROB-597"],["dc.relation.eissn","1879-6400"],["dc.relation.issn","1879-6397"],["dc.title","Huntingtin and Its Partner Huntingtin-Associated Protein 40: Structural and Functional Considerations in Health and Disease"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","534"],["dc.bibliographiccitation.issue","2"],["dc.bibliographiccitation.journal","Biochemical Society Transactions"],["dc.bibliographiccitation.lastpage","540"],["dc.bibliographiccitation.volume","44"],["dc.contributor.author","Fernández Busnadiego, Rubén"],["dc.date.accessioned","2022-03-01T11:46:16Z"],["dc.date.available","2022-03-01T11:46:16Z"],["dc.date.issued","2016"],["dc.description.abstract","The endoplasmic reticulum (ER) forms membrane contact sites (MCS) with most other cellular organelles and the plasma membrane (PM). These ER–PM MCS, where the membranes of the ER and PM are closely apposed, were discovered in the early days of electron microscopy (EM), but only recently are we starting to understand their functional and structural diversity. ER–PM MCS are nowadays known to mediate excitation–contraction coupling (ECC) in striated muscle cells and to play crucial roles in Ca2+ and lipid homoeostasis in all metazoan cells. A common feature across ER–PM MCS specialized in different functions is the preponderance of cooperative phenomena that result in the formation of large supramolecular assemblies. Therefore, characterizing the supramolecular architecture of ER–PM MCS is critical to understand their mechanisms of function. Cryo-electron tomography (cryo-ET) is a powerful EM technique uniquely positioned to address this issue, as it allows 3D imaging of fully hydrated, unstained cellular structures at molecular resolution. In this review I summarize our current structural knowledge on the molecular organization of ER–PM MCS and its functional implications, with special emphasis on the emerging contributions of cryo-ET."],["dc.description.abstract","The endoplasmic reticulum (ER) forms membrane contact sites (MCS) with most other cellular organelles and the plasma membrane (PM). These ER–PM MCS, where the membranes of the ER and PM are closely apposed, were discovered in the early days of electron microscopy (EM), but only recently are we starting to understand their functional and structural diversity. ER–PM MCS are nowadays known to mediate excitation–contraction coupling (ECC) in striated muscle cells and to play crucial roles in Ca2+ and lipid homoeostasis in all metazoan cells. A common feature across ER–PM MCS specialized in different functions is the preponderance of cooperative phenomena that result in the formation of large supramolecular assemblies. Therefore, characterizing the supramolecular architecture of ER–PM MCS is critical to understand their mechanisms of function. Cryo-electron tomography (cryo-ET) is a powerful EM technique uniquely positioned to address this issue, as it allows 3D imaging of fully hydrated, unstained cellular structures at molecular resolution. In this review I summarize our current structural knowledge on the molecular organization of ER–PM MCS and its functional implications, with special emphasis on the emerging contributions of cryo-ET."],["dc.identifier.doi","10.1042/BST20150279"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/103612"],["dc.language.iso","en"],["dc.notes.intern","DOI-Import GROB-531"],["dc.relation.eissn","1470-8752"],["dc.relation.issn","0300-5127"],["dc.title","Supramolecular architecture of endoplasmic reticulum–plasma membrane contact sites"],["dc.type","journal_article"],["dc.type.internalPublication","unknown"],["dspace.entity.type","Publication"]]

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[["dc.contributor.author","Riemenschneider, Henrick"],["dc.contributor.author","Guo, Qiang"],["dc.contributor.author","Bader, Jakob"],["dc.contributor.author","Frottin, Frédéric"],["dc.contributor.author","Farny, Daniel"],["dc.contributor.author","Kleinberger, Gernot"],["dc.contributor.author","Haass, Christian"],["dc.contributor.author","Mann, Matthias"],["dc.contributor.author","Hartl, F. Ulrich"],["dc.contributor.author","Baumeister, Wolfgang"],["dc.contributor.author","Hipp, Mark S."],["dc.contributor.author","Meissner, Felix"],["dc.contributor.author","Fernández Busnadiego, Rubén"],["dc.contributor.author","Edbauer, Dieter"],["dc.date.accessioned","2022-02-23T16:35:41Z"],["dc.date.available","2022-02-23T16:35:41Z"],["dc.date.issued","2021"],["dc.identifier.doi","10.1101/2021.03.15.435268"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/100379"],["dc.identifier.url","https://mbexc.uni-goettingen.de/literature/publications/288"],["dc.relation","EXC 2067: Multiscale Bioimaging"],["dc.relation.workinggroup","RG Fernández-Busnadiego (Structural Cell Biology)"],["dc.title","Gel-like inclusions of C-terminal fragments of TDP-43 sequester and inhibit proteasomes in neurons"],["dc.type","preprint"],["dc.type.internalPublication","unknown"],["dspace.entity.type","Publication"]]

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