Candiello, Ermes

[["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.artnumber","29950"],["dc.bibliographiccitation.journal","Scientific Reports"],["dc.bibliographiccitation.volume","6"],["dc.contributor.author","Candiello, Ermes"],["dc.contributor.author","Kratzke, Manuel"],["dc.contributor.author","Wenzel, Dirk"],["dc.contributor.author","Cassel, Dan"],["dc.contributor.author","Schu, Peter"],["dc.date.accessioned","2018-11-07T10:11:38Z"],["dc.date.available","2018-11-07T10:11:38Z"],["dc.date.issued","2016"],["dc.description.abstract","The sigma 1 subunit of the AP-1 clathrin-coated-vesicle adaptor-protein complex is expressed as three isoforms. Tissues express sigma 1A and one of the sigma 1B and sigma 1C isoforms. Brain is the tissue with the highest sigma 1A and sigma 1B expression. sigma 1B-deficiency leads to severe mental retardation, accumulation of early endosomes in synapses and fewer synaptic vesicles, whose recycling is slowed down. AP-1/sigma 1A and AP-1/sigma 1B regulate maturation of these early endosomes into multivesicular body late endosomes, thereby controlling synaptic vesicle protein transport into a degradative pathway. sigma 1A binds ArfGAP1, and with higher affinity brain-specific ArfGAP1, which bind Rabex-5. AP-1/sigma 1A-ArfGAP1-Rabex-5 complex formation leads to more endosomal Rabex-5 and enhanced, Rab5(GTP)-stimulated Vps34 PI3-kinase activity, which is essential for multivesicular body endosome formation. Formation of AP-1/sigma 1A-ArfGAP1-Rabex-5 complexes is prevented by sigma 1B binding of Rabex-5 and the amount of endosomal Rabex-5 is reduced. AP-1 complexes differentially regulate endosome maturation and coordinate protein recycling and degradation, revealing a novel molecular mechanism by which they regulate protein transport besides their established function in clathrin-coated-vesicle formation."],["dc.description.sponsorship","DFG [Schu 802/3-1, Schu 802/3-2, Schu 802/3-4]; GGNB grants"],["dc.identifier.doi","10.1038/srep29950"],["dc.identifier.isi","000379692700001"],["dc.identifier.pmid","27411398"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/13532"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/40086"],["dc.notes.intern","Merged from goescholar"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["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","AP-1/sigma 1A and AP-1/sigma 1B adaptor-proteins differentially regulate neuronal early endosome maturation via the Rab5/Vps34-pathway"],["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.firstpage","356"],["dc.bibliographiccitation.issue","4"],["dc.bibliographiccitation.journal","European Journal of Cell Biology"],["dc.bibliographiccitation.lastpage","368"],["dc.bibliographiccitation.volume","96"],["dc.contributor.author","Zizioli, Daniela"],["dc.contributor.author","Geumann, Constanze"],["dc.contributor.author","Kratzke, Manuel"],["dc.contributor.author","Mishra, Ratnakar"],["dc.contributor.author","Borsani, Guiseppe"],["dc.contributor.author","Finazzi, Dario"],["dc.contributor.author","Candiello, Ermes"],["dc.contributor.author","Schu, Peter"],["dc.date.accessioned","2018-11-07T10:22:53Z"],["dc.date.available","2018-11-07T10:22:53Z"],["dc.date.issued","2017"],["dc.description.abstract","gamma 2 adaptin is homologous to gamma 1, but is only expressed in vertebrates while gamma 1 is found in all eukaryotes. We know little about gamma 2 functions and their relation to gamma 1. gamma 1 is an adaptin of the heterotetrameric AP-1 complexes, which sort proteins in and do form clathrin-coated transport vesicles and they also regulate maturation of early endosomes. gamma 1 knockout mice develop only to blastocysts and thus gamma 2 does not compensate gamma 1-deficiency in development. gamma 2 has not been classified as a clathrin-coated vesicle adaptor protein in proteome analyses and functions for monomeric gamma 2 in endosomal protein sorting have been proposed, but adaptin interaction studies suggested formation of heterotetrameric AP-1/gamma 2 complexes. We detected gamma 2 at the trans-Golgi network, on peripheral vesicles and identified gamma 2 clathrin-coated vesicles in mice. Ubiquitous sigma 1A and tissue-specific sigma 1B adaptins bind gamma 2 and gamma 1. sigma 1B knockout in mice does not effect gamma 1/sigma 1A AP-1 levels, but gamma 2/sigma 1A AP-1 levels are increased in brain and adipocytes. Also gamma 2 is essential in development. In zebrafish AP-1/gamma 2 and AP-1/gamma 1 fulfill different, essential functions in brain and the vascular system. (C) 2017 Elsevier GmbH. All rights reserved."],["dc.identifier.doi","10.1016/j.ejcb.2017.03.008"],["dc.identifier.isi","000404504700007"],["dc.identifier.pmid","28372831"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/42353"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","PUB_WoS_Import"],["dc.publisher","Elsevier Gmbh, Urban & Fischer Verlag"],["dc.relation.issn","1618-1298"],["dc.relation.issn","0171-9335"],["dc.title","gamma 2 and gamma 1AP-1 complexes: Different essential functions and regulatory mechanisms in clathrin-dependent protein sorting"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["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.artnumber","8007"],["dc.bibliographiccitation.issue","1"],["dc.bibliographiccitation.journal","Scientific Reports"],["dc.bibliographiccitation.volume","11"],["dc.contributor.author","Mishra, R."],["dc.contributor.author","Sengül, G. F."],["dc.contributor.author","Candiello, E:"],["dc.contributor.author","Schu, P."],["dc.date.accessioned","2021-06-01T09:41:43Z"],["dc.date.available","2021-06-01T09:41:43Z"],["dc.date.issued","2021"],["dc.description.abstract","Abstract The AP1/σ1B knockout causes impaired synaptic vesicle recycling and enhanced protein sorting into endosomes, leading to severe intellectual disability. These disturbances in synaptic protein sorting induce as a secondary phenotype the upregulation of AP2 CCV mediated endocytosis. Synapses contain canonical AP2 CCV and AP2 CCV with a more stable coat and thus extended life time. In AP1/σ1B knockout synapses, pool sizes of both CCV classes are doubled. Additionally, stable CCV of the knockout are more stabilised than stable wt CCV. One mechanism responsible for enhanced CCV stabilisation is the reduction of synaptojanin1 CCV levels, the PI-4,5-P 2 phosphatase essential for AP2 membrane dissociation. To identify mechanisms regulating synaptojanin1 recruitment, we compared synaptojanin1 CCV protein interactome levels and CCV protein interactions between both CCV classes from wt and knockout mice. We show that ITSN1 determines synaptojanin1 CCV levels. Sgip1/AP2 excess hinders synaptojanin1 binding to ITSN1, further lowering its levels. ITSN1 levels are determined by Eps15, not Eps15L1. In addition, the data reveal that reduced amounts of pacsin1 can be counter balanced by its enhanced activation. These data exemplify the complexity of CCV life cycle regulation and indicate how cargo proteins determine the life cycle of their CCV."],["dc.description.sponsorship","Open-Access-Publikationsfonds 2021"],["dc.identifier.doi","10.1038/s41598-021-87591-3"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/85018"],["dc.language.iso","en"],["dc.notes.intern","DOI-Import GROB-425"],["dc.relation.eissn","2045-2322"],["dc.rights","CC BY 4.0"],["dc.title","Synaptic AP2 CCV life cycle regulation by the Eps15, ITSN1, Sgip1/AP2, synaptojanin1 interactome"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.subtype","original_ja"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]