Krinner, Stefanie

[["dc.bibliographiccitation.firstpage","6843"],["dc.bibliographiccitation.issue","20"],["dc.bibliographiccitation.journal","The Journal of neuroscience"],["dc.bibliographiccitation.lastpage","6848"],["dc.bibliographiccitation.volume","34"],["dc.contributor.author","Weiler, Simon"],["dc.contributor.author","Krinner, Stefanie"],["dc.contributor.author","Wong, Aaron B."],["dc.contributor.author","Moser, Tobias"],["dc.contributor.author","Pangršič, Tina"],["dc.date.accessioned","2017-09-07T11:46:15Z"],["dc.date.available","2017-09-07T11:46:15Z"],["dc.date.issued","2014"],["dc.description.abstract","Sound encoding is mediated by Ca2+ influx-evoked release of glutamate at the ribbon synapse of inner hair cells. Here we studied the role of ATP in this process focusing on Ca2+ current through Ca(V)1.3 channels and Ca2+ homeostasis in mouse inner hair cells. Patch-clamp recordings and Ca2+ imaging demonstrate that hydrolyzable ATP is essential to maintain synaptic Ca2+ influx in inner hair cells via fueling Ca2+-ATPases to avoid an increase in cytosolic [Ca2+] and subsequent Ca2+/calmodulin-dependent inactivation of Ca(V)1.3 channels."],["dc.identifier.doi","10.1523/JNEUROSCI.4990-13.2014"],["dc.identifier.gro","3142124"],["dc.identifier.isi","000336895000012"],["dc.identifier.pmid","24828638"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/4811"],["dc.notes.intern","WoS Import 2017-03-10"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.publisher","Soc Neuroscience"],["dc.relation.issn","0270-6474"],["dc.title","ATP Hydrolysis Is Critically Required for Function of Ca(V)1.3 Channels in Cochlear Inner Hair Cells via Fueling Ca2+ Clearance"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.artnumber","651935"],["dc.bibliographiccitation.journal","Frontiers in Molecular Neuroscience"],["dc.bibliographiccitation.volume","14"],["dc.contributor.author","Burfeind, Dinah"],["dc.contributor.author","Moser, Tobias"],["dc.contributor.author","Krinner, Stefanie"],["dc.contributor.author","Predoehl, Friederike"],["dc.contributor.author","Vogl, Christian"],["dc.date.accessioned","2021-04-29T08:36:41Z"],["dc.date.available","2021-04-29T08:36:41Z"],["dc.date.issued","2021"],["dc.description.abstract","The afferent synapses between inner hair cells (IHC) and spiral ganglion neurons are specialized to faithfully encode sound with sub-millisecond precision over prolonged periods of time. Here, we studied the role of Rab3 interacting molecule-binding proteins (RIM-BP) 1 and 2 - multidomain proteins of the active zone known to directly interact with RIMs, Bassoon and Ca V 1.3 - in IHC presynaptic function and hearing. Recordings of auditory brainstem responses and otoacoustic emissions revealed that genetic disruption of RIM-BPs 1 and 2 in mice (RIM-BP1/2-/- ) causes a synaptopathic hearing impairment exceeding that found in mice lacking RIM-BP2 (RIM-BP2-/- ). Patch-clamp recordings from RIM-BP1/2-/- IHCs indicated a subtle impairment of exocytosis from the readily releasable pool of synaptic vesicles that had not been observed in RIM-BP2-/- IHCs. In contrast, the reduction of Ca2+-influx and sustained exocytosis was similar to that in RIMBP2-/- IHCs. We conclude that both RIM-BPs are required for normal sound encoding at the IHC synapse, whereby RIM-BP2 seems to take the leading role."],["dc.identifier.doi","10.3389/fnmol.2021.651935"],["dc.identifier.pmid","33867935"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/84562"],["dc.identifier.url","https://mbexc.uni-goettingen.de/literature/publications/237"],["dc.identifier.url","https://sfb1286.uni-goettingen.de/literature/publications/114"],["dc.language.iso","en"],["dc.notes.intern","DeepGreen Import"],["dc.relation","EXC 2067: Multiscale Bioimaging"],["dc.relation","SFB 1286: Quantitative Synaptologie"],["dc.relation","SFB 1286 | B05: Quantitative molekulare Physiologie aktiver Zonen in Calyx-Synapsen"],["dc.relation.eissn","1662-5099"],["dc.relation.issn","1662-5099"],["dc.relation.workinggroup","RG Moser (Molecular Anatomy, Physiology and Pathology of Sound Encoding)"],["dc.rights","http://creativecommons.org/licenses/by/4.0/"],["dc.title","RIM-Binding Proteins Are Required for Normal Sound-Encoding at Afferent Inner Hair Cell Synapses"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.subtype","original_ja"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.artnumber","334"],["dc.bibliographiccitation.journal","Frontiers in Cellular Neuroscience"],["dc.bibliographiccitation.volume","11"],["dc.contributor.author","Krinner, Stefanie"],["dc.contributor.author","Butola, Tanvi"],["dc.contributor.author","Jung, SangYong"],["dc.contributor.author","Wichmann, Carolin"],["dc.contributor.author","Moser, Tobias"],["dc.date.accessioned","2018-01-17T11:39:13Z"],["dc.date.available","2018-01-17T11:39:13Z"],["dc.date.issued","2017"],["dc.description.abstract","Ribbon synapses of inner hair cells (IHCs) mediate high rates of synchronous exocytosis to indefatigably track the stimulating sound with sub-millisecond precision. The sophisticated molecular machinery of the inner hair cell active zone realizes this impressive performance by enabling a large number of synaptic voltage-gated CaV1.3 Ca2+-channels, their tight coupling to synaptic vesicles (SVs) and fast replenishment of fusion competent SVs. Here we studied the role of RIM-binding protein 2 (RIM-BP2)-a multidomain cytomatrix protein known to directly interact with Rab3 interacting molecules (RIMs), bassoon and CaV1.3-that is present at the inner hair cell active zones. We combined confocal and stimulated emission depletion (STED) immunofluorescence microscopy, electron tomography, patch-clamp and confocal Ca2+-imaging, as well as auditory systems physiology to explore the morphological and functional effects of genetic RIM-BP2 disruption in constitutive RIM-BP2 knockout mice. We found that RIM-BP2 (1) positively regulates the number of synaptic CaV1.3 channels and thereby facilitates synaptic vesicle release and (2) supports fast synaptic vesicle recruitment after readily releasable pool (RRP) depletion. However, Ca2+-influx-exocytosis coupling seemed unaltered for readily releasable SVs. Recordings of auditory brainstem responses (ABR) and of single auditory nerve fiber firing showed that RIM-BP2 disruption results in a mild deficit of synaptic sound encoding."],["dc.format.extent","1"],["dc.identifier.doi","10.3389/fncel.2017.00334"],["dc.identifier.pmid","29163046"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/14890"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/11684"],["dc.identifier.url","https://sfb1286.uni-goettingen.de/literature/publications/30"],["dc.language.iso","en"],["dc.notes.intern","Merged from goescholar"],["dc.notes.status","final"],["dc.relation","SFB 1286: Quantitative Synaptologie"],["dc.relation","SFB 1286 | A04: Aktivitätsabhängige morphologische Veränderungen am Endkolben von Held-Synapsen"],["dc.relation","SFB 1286 | B05: Quantitative molekulare Physiologie aktiver Zonen in Calyx-Synapsen"],["dc.relation.workinggroup","RG Moser (Molecular Anatomy, Physiology and Pathology of Sound Encoding)"],["dc.relation.workinggroup","RG Wichmann (Molecular Architecture of Synapses)"],["dc.rights","CC BY 4.0"],["dc.rights.uri","https://creativecommons.org/licenses/by/4.0"],["dc.title","RIM-Binding Protein 2 Promotes a Large Number of CaV1.3 Ca2+-Channels and Contributes to Fast Synaptic Vesicle Replenishment at Hair Cell Active Zones"],["dc.type","journal_article"],["dc.type.internalPublication","unknown"],["dc.type.subtype","original_ja"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]