Schmidt, Bernhard

[["dc.bibliographiccitation.firstpage","142"],["dc.bibliographiccitation.issue","1"],["dc.bibliographiccitation.journal","Molecular Neurobiology"],["dc.bibliographiccitation.lastpage","161"],["dc.bibliographiccitation.volume","52"],["dc.contributor.author","Kratzke, Manuel"],["dc.contributor.author","Candiello, Ermes"],["dc.contributor.author","Schmidt, Bernhard"],["dc.contributor.author","Jahn, Olaf"],["dc.contributor.author","Schu, Peter"],["dc.date.accessioned","2018-11-07T09:54:05Z"],["dc.date.available","2018-11-07T09:54:05Z"],["dc.date.issued","2015"],["dc.description.abstract","Adaptor protein (AP)-1/sigma 1B(-/-) mice have reduced synaptic-vesicle (SV) recycling and increased endosomes. Mutant mice have impaired spatial memory, and sigma 1B-deficient humans have a severe mental retardation. In order to define these sigma 1B(-/-) 'bulk' endosomes and to determine their functions in SV recycling, we developed a protocol to separate them from the majority of the neuronal endosomes. The sigma 1B(-/-) 'bulk' endosomes proved to be classic early endosomes with an increase in the phospholipid phosphatidylinositol 3-phosphate (PI-3-P), which recruits proteins mediating protein sorting out of early endosomes into different routes. sigma 1B deficiency induced alterations in the endosomal proteome reveals two major functions: SV protein storage and sorting into endolysosomes. Alternative endosomal recycling pathways are not up-regulated, but certain SV proteins are misrouted. Tetraspanins are enriched in sigma 1B(-/-) synaptosomes, but not in their endosomes or in their clathrin-coated-vesicles (CCVs), indicating AP-1/sigma 1B-dependent sorting. Synapses contain also more AP-2 CCV, although it is expected that they contain less due to reduced SV recycling. Coat composition of these AP-2 CCVs is altered, and thus, they represent a subpopulation of AP-2 CCVs. Association of calmodulin-dependent protein kinase (CaMK)-II alpha, -delta and casein kinase (CK)-II alpha with the endosome/SV pool is altered, as well as 14-3-3 eta, indicating changes in specific signalling pathways regulating synaptic plasticity. The accumulation of early endosomes and endocytotic AP-2 CCV indicates the regulation of SV recycling via early endosomes by the interdependent regulation of AP-2-mediated endocytosis and AP-1/sigma 1B-mediated SV reformation."],["dc.description.sponsorship","DFG [Schu 802/3-1, 802/3-2]"],["dc.identifier.doi","10.1007/s12035-014-8852-0"],["dc.identifier.isi","000358341600014"],["dc.identifier.pmid","25128028"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/36465"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Humana Press Inc"],["dc.relation.issn","1559-1182"],["dc.relation.issn","0893-7648"],["dc.title","AP-1/sigma 1B-Dependent SV Protein Recycling Is Regulated in Early Endosomes and Is Coupled to AP-2 Endocytosis"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","643"],["dc.bibliographiccitation.issue","4"],["dc.bibliographiccitation.journal","The Journal of Cell Biology"],["dc.bibliographiccitation.lastpage","656"],["dc.bibliographiccitation.volume","195"],["dc.contributor.author","Schulz, Christian"],["dc.contributor.author","Lytovchenko, Oleksandr"],["dc.contributor.author","Melin, Jonathan"],["dc.contributor.author","Chacinska, Agnieszka"],["dc.contributor.author","Guiard, Bernard"],["dc.contributor.author","Neumann, Piotr"],["dc.contributor.author","Ficner, Ralf"],["dc.contributor.author","Jahn, Olaf"],["dc.contributor.author","Schmidt, Bernhard"],["dc.contributor.author","Rehling, Peter"],["dc.date.accessioned","2017-09-07T11:43:19Z"],["dc.date.available","2017-09-07T11:43:19Z"],["dc.date.issued","2011"],["dc.description.abstract","N-terminal targeting signals (presequences) direct proteins across the TOM complex in the outer mitochondrial membrane and the TIM23 complex in the inner mitochondrial membrane. Presequences provide directionality to the transport process and regulate the transport machineries during translocation. However, surprisingly little is known about how presequence receptors interact with the signals and what role these interactions play during preprotein transport. Here, we identify signal-binding sites of presequence receptors through photo-affinity labeling. Using engineered presequence probes, photo cross-linking sites on mitochondrial proteins were mapped mass spectrometrically, thereby defining a presequence-binding domain of Tim50, a core subunit of the TIM23 complex that is essential for mitochondrial protein import. Our results establish Tim50 as the primary presequence receptor at the inner membrane and show that targeting signals and Tim50 regulate the Tim23 channel in an antagonistic manner."],["dc.identifier.doi","10.1083/jcb.201105098"],["dc.identifier.gro","3142630"],["dc.identifier.isi","000297206400012"],["dc.identifier.pmid","22065641"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/8033"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/55"],["dc.notes.intern","WoS Import 2017-03-10"],["dc.notes.intern","Merged from goescholar"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.publisher","Rockefeller Univ Press"],["dc.relation.issn","0021-9525"],["dc.rights","Goescholar"],["dc.rights.uri","https://goescholar.uni-goettingen.de/licenses"],["dc.title","Tim50's presequence receptor domain is essential for signal driven transport across the TIM23 complex"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","3473"],["dc.bibliographiccitation.issue","18"],["dc.bibliographiccitation.journal","Molecular and Cellular Biology"],["dc.bibliographiccitation.lastpage","3485"],["dc.bibliographiccitation.volume","34"],["dc.contributor.author","Melin, Jonathan"],["dc.contributor.author","Schulz, Christian"],["dc.contributor.author","Wrobel, Lidia"],["dc.contributor.author","Bernhard, Olaf"],["dc.contributor.author","Chacinska, Agnieszka"],["dc.contributor.author","Jahn, Olaf"],["dc.contributor.author","Schmidt, Bernhard"],["dc.contributor.author","Rehling, Peter"],["dc.date.accessioned","2017-09-07T11:45:36Z"],["dc.date.available","2017-09-07T11:45:36Z"],["dc.date.issued","2014"],["dc.description.abstract","More than 70% of mitochondrial proteins utilize N-terminal presequences as targeting signals. Presequence interactions with redundant cytosolic receptor domains of the translocase of the outer mitochondrial membrane (TOM) are well established. However, after the presequence enters the protein-conducting Tom40 channel, the recognition events that occur at the trans side leading up to the engagement of the presequence with inner membrane-bound receptors are less well defined. Using a photoaffinity-labeling approach with modified presequence peptides, we identified Tom40 as a presequence interactor of the TOM complex. Utilizing mass spectrometry, we mapped Tom40's presequence-interacting regions to both sides of the beta-barrel. Analysis of a phosphorylation site within one of the presequence-interacting regions revealed altered translocation kinetics along the presequence pathway. Our analyses assess the relation between the identified presequence-binding region of Tom40 and the intermembrane space domain of Tom22. The identified presequence-interacting region of Tom40 is capable of functioning independently of the established trans-acting TOM presequence-binding domain during matrix import."],["dc.identifier.doi","10.1128/MCB.00433-14"],["dc.identifier.gro","3142065"],["dc.identifier.isi","000341024900010"],["dc.identifier.pmid","25002531"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/4156"],["dc.language.iso","en"],["dc.notes.intern","WoS Import 2017-03-10"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.relation.eissn","1098-5549"],["dc.relation.issn","0270-7306"],["dc.title","Presequence Recognition by the Tom40 Channel Contributes to Precursor Translocation into the Mitochondrial Matrix"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","1192"],["dc.bibliographiccitation.issue","10"],["dc.bibliographiccitation.journal","Cells"],["dc.bibliographiccitation.volume","8"],["dc.contributor.author","Beißbarth, Tim"],["dc.contributor.author","Bohrer, Rainer"],["dc.contributor.author","Feussner, Kirstin"],["dc.contributor.author","Jahn, Olaf"],["dc.contributor.author","Schmitt, Kerstin"],["dc.contributor.author","Valerius, Oliver"],["dc.contributor.author","Asif, Abdul R."],["dc.contributor.author","Dihazi, Hassan"],["dc.contributor.author","Majcherczyk, Andrzej"],["dc.contributor.author","Schmidt, Bernhard"],["dc.contributor.author","Urlaub, Henning"],["dc.contributor.author","Lenz, Christof"],["dc.date.accessioned","2020-04-02T10:32:12Z"],["dc.date.available","2020-04-02T10:32:12Z"],["dc.date.issued","2019"],["dc.description.abstract","Mass spectrometry-based proteomics methods are finding increasing use in structural biology research. Beyond simple interaction networks, information about stable protein-protein complexes or spatially proximal proteins helps to elucidate the biological functions of proteins in a wider cellular context. To shed light on new developments in this field, the Göttingen Proteomics Forum organized a one-day symposium focused on complexome profiling and proximity labeling, two emerging technologies that are gaining significant attention in biomolecular research. The symposium was held in Göttingen, Germany on 23 May, 2019, as part of a series of regular symposia organized by the Göttingen Proteomics Forum."],["dc.identifier.doi","10.3390/cells8101192"],["dc.identifier.pmid","31581721"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/16914"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/63512"],["dc.identifier.url","https://sfb1190.med.uni-goettingen.de/production/literature/publications/95"],["dc.language.iso","en"],["dc.notes.intern","Merged from goescholar"],["dc.publisher","MDPI"],["dc.relation","SFB 1190: Transportmaschinen und Kontaktstellen zellulärer Kompartimente"],["dc.relation","SFB 1190 | Z02: Massenspektrometrie-basierte Proteomanalyse"],["dc.relation.conference","Seventh Symposium of the Göttingen Proteomics Forum"],["dc.relation.eissn","2073-4409"],["dc.relation.eventlocation","Göttingen"],["dc.relation.eventstart","2019-05-23"],["dc.relation.issn","2073-4409"],["dc.relation.orgunit","Gesellschaft für wissenschaftliche Datenverarbeitung"],["dc.relation.workinggroup","RG Urlaub (Bioanalytische Massenspektrometrie)"],["dc.rights","CC BY 4.0"],["dc.rights.uri","https://creativecommons.org/licenses/by/4.0"],["dc.title","Mapping Cellular Microenvironments: Proximity Labeling and Complexome Profiling"],["dc.type","conference_paper"],["dc.type.internalPublication","yes"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.artnumber","15781"],["dc.bibliographiccitation.issue","1"],["dc.bibliographiccitation.journal","Scientific Reports"],["dc.bibliographiccitation.volume","7"],["dc.contributor.author","Candiello, Ermes"],["dc.contributor.author","Mishra, Ratnakar"],["dc.contributor.author","Schmidt, Bernhard"],["dc.contributor.author","Jahn, Olaf"],["dc.contributor.author","Schu, Peter"],["dc.date.accessioned","2019-07-09T11:44:40Z"],["dc.date.available","2019-07-09T11:44:40Z"],["dc.date.issued","2017-11-17"],["dc.description.abstract","AP-1/σ1B-deficiency causes X-linked intellectual disability. AP-1/σ1B -/- mice have impaired synaptic vesicle recycling, fewer synaptic vesicles and enhanced endosome maturation mediated by AP-1/σ1A. Despite defects in synaptic vesicle recycling synapses contain two times more endocytic AP-2 clathrin-coated vesicles. We demonstrate increased formation of two classes of AP-2/clathrin coated vesicles. One which uncoats readily and a second with a stabilised clathrin coat. Coat stabilisation is mediated by three molecular mechanisms: reduced recruitment of Hsc70 and synaptojanin1 and enhanced μ2/AP-2 phosphorylation and activation. Stabilised AP-2 vesicles are enriched in the structural active zone proteins Git1 and stonin2 and synapses contain more Git1. Endocytosis of the synaptic vesicle exocytosis regulating Munc13 isoforms are differentially effected. Regulation of synaptic protein endocytosis by the differential stability of AP-2/clathrin coats is a novel molecular mechanism of synaptic plasticity."],["dc.identifier.doi","10.1038/s41598-017-16055-4"],["dc.identifier.pmid","29150658"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/14858"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/59063"],["dc.language.iso","en"],["dc.notes.intern","Merged from goescholar"],["dc.relation.issn","2045-2322"],["dc.rights","CC BY 4.0"],["dc.rights.uri","https://creativecommons.org/licenses/by/4.0"],["dc.subject.ddc","610"],["dc.title","Differential regulation of synaptic AP-2/clathrin vesicle uncoating in synaptic plasticity."],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","1850"],["dc.bibliographiccitation.issue","8"],["dc.bibliographiccitation.journal","Biochimica et Biophysica Acta (BBA) - Molecular Cell Research"],["dc.bibliographiccitation.lastpage","1859"],["dc.bibliographiccitation.volume","1853"],["dc.contributor.author","Melin, Jonathan"],["dc.contributor.author","Kilisch, Markus"],["dc.contributor.author","Neumann, Piotr"],["dc.contributor.author","Lytovchenko, Oleksandr"],["dc.contributor.author","Gomkale, Ridhima"],["dc.contributor.author","Schendzielorz, Alexander Benjamin"],["dc.contributor.author","Schmidt, Bernhard"],["dc.contributor.author","Liepold, Thomas"],["dc.contributor.author","Ficner, Ralf"],["dc.contributor.author","Jahn, Olaf"],["dc.contributor.author","Rehling, Peter"],["dc.contributor.author","Schulz, Christian"],["dc.date.accessioned","2017-09-07T11:43:40Z"],["dc.date.available","2017-09-07T11:43:40Z"],["dc.date.issued","2015"],["dc.description.abstract","The translocase of the outer mitochondrial membrane (TOM complex) is the general entry gate into mitochondria for almost all imported proteins. A variety of specific receptors allow the TOM complex to recognize targeting signals of various precursor proteins that are transported along different import pathways. Aside from the well-characterized presequence receptors Tom20 and Tom22 a third TOM receptor, Tom70, binds proteins of the carrier family containing multiple transmembrane segments. Here we demonstrate that Tom70 directly binds to presequence peptides using a dedicated groove. A single point mutation in the cavity of this pocket (M551R) reduces the presequence binding affinity of Tom70 ten-fold and selectively impairs import of the presequence-containing precursor Mdl1 but not the ADP/ATP carrier (MC). Hence Tom70 contributes to the presequence import pathway by recognition of the targeting signal of the Mdl1 precursor. (C) 2015 Elsevier B.V. All rights reserved."],["dc.identifier.doi","10.1016/j.bbamcr.2015.04.021"],["dc.identifier.gro","3141858"],["dc.identifier.isi","000356209600009"],["dc.identifier.pmid","25958336"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/1856"],["dc.language.iso","en"],["dc.notes.intern","WoS Import 2017-03-10"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.relation.eissn","0006-3002"],["dc.relation.issn","0167-4889"],["dc.title","A presequence-binding groove in Tom70 supports import of Mdl1 into mitochondria"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","17"],["dc.bibliographiccitation.issue","1"],["dc.bibliographiccitation.journal","Expert Review of Proteomics"],["dc.bibliographiccitation.lastpage","20"],["dc.bibliographiccitation.volume","10"],["dc.contributor.author","Dihazi, Hassan"],["dc.contributor.author","Bohrer, Rainer"],["dc.contributor.author","Jahn, Olaf"],["dc.contributor.author","Lenz, Christof"],["dc.contributor.author","Majcherczyk, Andrzej"],["dc.contributor.author","Schmidt, Bernhard"],["dc.contributor.author","Urlaub, Henning"],["dc.contributor.author","Valerius, Oliver"],["dc.contributor.author","Asif, Abdul R"],["dc.date.accessioned","2021-06-01T10:48:27Z"],["dc.date.available","2021-06-01T10:48:27Z"],["dc.date.issued","2013"],["dc.description.abstract","Advances in Bioanalytical Mass Spectrometry: 5th Symposium of the Gottingen Proteomics Forum Mass Spectrometry with Spatial Resolution: MALDI-Imaging and Laser Capture Microscopy Gottingen, Germany, 22 November 2012 MALDI mass spectrometry imaging (MSI) combines the speed and molecular specificity of MALDI-MS detection with information on spatial organization. In the last years, MSI found large application in proteomics research for determining the spatial distribution of compounds in biological tissues and started to draw increasing interest in clinical research. To shed light on the new developments in the field of MSI, the Gottingen Proteomics Forum organized a symposium that was held in Gottingen as part of the series of regular symposia organized by the members of the Gottingen Proteomics Forum. The symposium was on 22 November 2012, with more than 80 delegates that attended the event entitled 'Mass spectrometry with spatial resolution: MALDI-imaging and laser capture microscopy'. The one-day agenda consisted of nine oral presentations from renowned experts in the field with subsequent discussion sessions. As usual, the meeting was fruitful and offered a good platform for discussion between the delegates and proteomics specialists."],["dc.identifier.doi","10.1586/epr.12.73"],["dc.identifier.isi","000315163000010"],["dc.identifier.pmid","23414355"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/85944"],["dc.language.iso","en"],["dc.notes.intern","DOI-Import GROB-425"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.relation.eissn","1744-8387"],["dc.relation.issn","1478-9450"],["dc.relation.orgunit","Gesellschaft für wissenschaftliche Datenverarbeitung"],["dc.title","Mass spectrometry imaging: linking molecule profiles to tissue spatial distribution"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original_ja"],["dspace.entity.type","Publication"]]