Schu, Peter Valentin

[["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","5274"],["dc.bibliographiccitation.issue","10"],["dc.bibliographiccitation.journal","International Journal of Molecular Sciences"],["dc.bibliographiccitation.volume","22"],["dc.contributor.affiliation","Strazic Geljic, Ivana; \t\t \r\n\t\t Center for Proteomics, Faculty of Medicine, University of Rijeka, 51000 Rijeka, Croatia, Ivana.StrazicGeljic@fidelta.eu\t\t \r\n\t\t Fidelta Ltd., Prilaz baruna Filipovica 29, 10000 Zagreb, Croatia, Ivana.StrazicGeljic@fidelta.eu"],["dc.contributor.affiliation","Kucan Brlic, Paola; \t\t \r\n\t\t Center for Proteomics, Faculty of Medicine, University of Rijeka, 51000 Rijeka, Croatia, paola.kucan@medri.uniri.hr\t\t \r\n\t\t Department of Histology and Embryology, Faculty of Medicine, University of Rijeka, 51000 Rijeka, Croatia, paola.kucan@medri.uniri.hr"],["dc.contributor.affiliation","Musak, Lucija; \t\t \r\n\t\t Fidelta Ltd., Prilaz baruna Filipovica 29, 10000 Zagreb, Croatia, Lucija.Musak@fidelta.eu"],["dc.contributor.affiliation","Karner, Dubravka; \t\t \r\n\t\t Center for Proteomics, Faculty of Medicine, University of Rijeka, 51000 Rijeka, Croatia, dubravka.karner@medri.uniri.hr"],["dc.contributor.affiliation","Ambriović-Ristov, Andreja; \t\t \r\n\t\t Laboratory for Cell Biology and Signalling, Division of Molecular Biology, Ruđer Bošković Institute, Bijenička 54, 10000 Zagreb, Croatia, Andreja.Ambriovic.Ristov@irb.hr"],["dc.contributor.affiliation","Jonjic, Stipan; \t\t \r\n\t\t Center for Proteomics, Faculty of Medicine, University of Rijeka, 51000 Rijeka, Croatia, stipan.jonjic@medri.uniri.hr\t\t \r\n\t\t Department of Histology and Embryology, Faculty of Medicine, University of Rijeka, 51000 Rijeka, Croatia, stipan.jonjic@medri.uniri.hr"],["dc.contributor.affiliation","Schu, Peter; \t\t \r\n\t\t Department of Cellular Biochemistry, University Medical Center, Georg-August-University Göttingen, Humboldtallee 23, D-37073 Göttingen, Germany, pschu@gwdg.de"],["dc.contributor.affiliation","Rovis, Tihana Lenac; \t\t \r\n\t\t Center for Proteomics, Faculty of Medicine, University of Rijeka, 51000 Rijeka, Croatia, tihana.lenac@uniri.hr"],["dc.contributor.author","Strazic Geljic, Ivana"],["dc.contributor.author","Kucan Brlic, Paola"],["dc.contributor.author","Musak, Lucija"],["dc.contributor.author","Karner, Dubravka"],["dc.contributor.author","Ambriović-Ristov, Andreja"],["dc.contributor.author","Jonjic, Stipan"],["dc.contributor.author","Schu, Peter"],["dc.contributor.author","Rovis, Tihana Lenac"],["dc.date.accessioned","2021-07-05T15:00:46Z"],["dc.date.available","2021-07-05T15:00:46Z"],["dc.date.issued","2021"],["dc.date.updated","2022-09-06T07:02:16Z"],["dc.description.abstract","Numerous viruses hijack cellular protein trafficking pathways to mediate cell entry or to rearrange membrane structures thereby promoting viral replication and antagonizing the immune response. Adaptor protein complexes (AP), which mediate protein sorting in endocytic and secretory transport pathways, are one of the conserved viral targets with many viruses possessing AP-interacting motifs. We present here different mechanisms of viral interference with AP complexes and the functional consequences that allow for efficient viral propagation and evasion of host immune defense. The ubiquity of this phenomenon is evidenced by the fact that there are representatives for AP interference in all major viral families, covered in this review. The best described examples are interactions of human immunodeficiency virus and human herpesviruses with AP complexes. Several other viruses, like Ebola, Nipah, and SARS-CoV-2, are pointed out as high priority disease-causative agents supporting the need for deeper understanding of virus-AP interplay which can be exploited in the design of novel antiviral therapies."],["dc.description.abstract","Numerous viruses hijack cellular protein trafficking pathways to mediate cell entry or to rearrange membrane structures thereby promoting viral replication and antagonizing the immune response. Adaptor protein complexes (AP), which mediate protein sorting in endocytic and secretory transport pathways, are one of the conserved viral targets with many viruses possessing AP-interacting motifs. We present here different mechanisms of viral interference with AP complexes and the functional consequences that allow for efficient viral propagation and evasion of host immune defense. The ubiquity of this phenomenon is evidenced by the fact that there are representatives for AP interference in all major viral families, covered in this review. The best described examples are interactions of human immunodeficiency virus and human herpesviruses with AP complexes. Several other viruses, like Ebola, Nipah, and SARS-CoV-2, are pointed out as high priority disease-causative agents supporting the need for deeper understanding of virus-AP interplay which can be exploited in the design of novel antiviral therapies."],["dc.identifier.doi","10.3390/ijms22105274"],["dc.identifier.pii","ijms22105274"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/87897"],["dc.language.iso","en"],["dc.notes.intern","DOI Import DOI-Import GROB-441"],["dc.relation.eissn","1422-0067"],["dc.rights","CC BY 4.0"],["dc.rights.uri","https://creativecommons.org/licenses/by/4.0/"],["dc.title","Viral Interactions with Adaptor-Protein Complexes: A Ubiquitous Trait among Viral Species"],["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","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"]]

[["dc.bibliographiccitation.artnumber","1813"],["dc.bibliographiccitation.journal","Scientific Reports"],["dc.bibliographiccitation.volume","3"],["dc.contributor.author","Agrawal, Tanvi"],["dc.contributor.author","Schu, Peter"],["dc.contributor.author","Medigeshi, Guruprasad R."],["dc.date.accessioned","2018-11-07T09:24:43Z"],["dc.date.available","2018-11-07T09:24:43Z"],["dc.date.issued","2013"],["dc.description.abstract","Intracellular protein trafficking pathways are hijacked by viruses at various stages of viral life-cycle. Heterotetrameric adaptor protein complexes (APs) mediate vesicular trafficking at distinct intracellular sites and are essential for maintaining the organellar homeostasis. In the present study, we studied the effect of AP-1 and AP-3 deficiency on flavivirus infection in cells functionally lacking these proteins. We show that AP-1 and AP-3 participate in flavivirus life-cycle at distinct stages. AP-3-deficient cells showed delay in initiation of Japanese encephalitis virus and dengue virus RNA replication, which resulted in reduction of infectious virus production. AP-3 was found to colocalize with RNA replication compartments in infected wild-type cells. AP-1 deficiency affected later stages of dengue virus infection where increased intracellular accumulation of infectious virus was observed. Therefore, our results propose a novel role for AP-1 and AP-3 at distinct stages of infection of some of the RNA viruses."],["dc.description.sponsorship","vaccine research innovation award; Department of Biotechnology"],["dc.identifier.doi","10.1038/srep01813"],["dc.identifier.isi","000318572700003"],["dc.identifier.pmid","23657274"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/10731"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/29893"],["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-NC-ND 3.0"],["dc.rights.uri","https://creativecommons.org/licenses/by-nc-nd/3.0"],["dc.title","Adaptor protein complexes-1 and 3 are involved at distinct stages of flavivirus life-cycle"],["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"]]