Krick, Roswitha

[["dc.bibliographiccitation.firstpage","E2042"],["dc.bibliographiccitation.issue","30"],["dc.bibliographiccitation.journal","Proceedings of the National Academy of Sciences of the United States of America"],["dc.bibliographiccitation.lastpage","E2049"],["dc.bibliographiccitation.volume","109"],["dc.contributor.author","Krick, Roswitha"],["dc.contributor.author","Busse, Ricarda A."],["dc.contributor.author","Scacioc, Andreea"],["dc.contributor.author","Stephan, Milena"],["dc.contributor.author","Janshoff, Andreas"],["dc.contributor.author","Thumm, Michael"],["dc.contributor.author","Kuehnel, Karin"],["dc.date.accessioned","2018-11-07T09:08:09Z"],["dc.date.available","2018-11-07T09:08:09Z"],["dc.date.issued","2012"],["dc.description.abstract","beta-propellers that bind polyphosphoinositides (PROPPINs), a eukaryotic WD-40 motif-containing protein family, bind via their predicted beta-propeller fold the polyphosphoinositides PtdIns3P and PtdIns(3,5) P-2 using a conserved FRRG motif. PROPPINs play a key role in macroautophagy in addition to other functions. We present the 3.0-angstrom crystal structure of Kluyveromyces lactis Hsv2, which shares significant sequence homologies with its three Saccharomyces cerevisiae homologs Atg18, Atg21, and Hsv2. It adopts a seven-bladed beta-propeller fold with a rare nonvelcro propeller closure. Remarkably, in the crystal structure, the two arginines of the FRRG motif are part of two distinct basic pockets formed by a set of highly conserved residues. In comprehensive in vivo and in vitro studies of ScAtg18 and ScHsv2, we define within the two pockets a set of conserved residues essential for normal membrane association, phosphoinositide binding, and biological activities. Our experiments show that PROPPINs contain two individual phosphoinositide binding sites. Based on docking studies, we propose a model for phosphoinositide binding of PROPPINs."],["dc.description.sponsorship","Deutsche Forschungsgemeinschaft [SFB860]"],["dc.identifier.doi","10.1073/pnas.1205128109"],["dc.identifier.isi","000306992700006"],["dc.identifier.pmid","22753491"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/25961"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Natl Acad Sciences"],["dc.relation.issn","0027-8424"],["dc.title","Structural and functional characterization of the two phosphoinositide binding sites of PROPPINs, a beta-propeller protein family"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","2223"],["dc.bibliographiccitation.issue","9"],["dc.bibliographiccitation.journal","Biophysical Journal"],["dc.bibliographiccitation.lastpage","2234"],["dc.bibliographiccitation.volume","108"],["dc.contributor.author","Busse, Ricarda A."],["dc.contributor.author","Scacioc, Andreea"],["dc.contributor.author","Krick, Roswitha"],["dc.contributor.author","Perez-Lara, Angel"],["dc.contributor.author","Thumm, Michael"],["dc.contributor.author","Kuehnel, Karin"],["dc.date.accessioned","2018-11-07T09:57:21Z"],["dc.date.available","2018-11-07T09:57:21Z"],["dc.date.issued","2015"],["dc.description.abstract","PROPPINs (beta-propellers that bind polyphosphoinositides) are a family of PtdIns3P- and PtdIns(3,5)P-2-binding proteins that play an important role in autophagy. We analyzed PROPPIN-membrane binding through isothermal titration calorimetry (ITC), stopped-flow measurements, mutagenesis studies, and molecular dynamics (MD) simulations. ITC measurements showed that the yeast PROPPIN family members Atg18, Atg21, and Hsv2 bind PtdIns3P and PtdIns(3,5)P-2 with high affinities in the nanomolar to low-micromolar range and have two phosphoinositide (PIP)-binding sites. Single PIP-binding site mutants have a 15- to 30-fold reduced affinity, which explains the requirement of two PIP-binding sites in PROPPINs. Hsv2 bound small unilamellar vesicles with a higher affinity than it bound large unilamellar vesicles in stopped-flow measurements. Thus, we conclude that PROPPIN membrane binding is curvature dependent. MD simulations revealed that loop 6CD is an anchor for membrane binding, as it is the region of the protein that inserts most deeply into the lipid bilayer. Mutagenesis studies showed that both hydrophobic and electrostatic interactions are required for membrane insertion of loop 6CD. We propose a model for PROPPIN-membrane binding in which PROPPINs are initially targeted to membranes through nonspecific electrostatic interactions and are then retained at the membrane through PIP binding."],["dc.description.sponsorship","DFG [SFB860]"],["dc.identifier.doi","10.1016/j.bpj.2015.03.045"],["dc.identifier.isi","000353986900017"],["dc.identifier.pmid","25954880"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/37138"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Cell Press"],["dc.relation.issn","1542-0086"],["dc.relation.issn","0006-3495"],["dc.title","Characterization of PROPPIN-Phosphoinositide Binding and Role of Loop 6CD in PROPPIN-Membrane Binding"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","1546"],["dc.bibliographiccitation.issue","12"],["dc.bibliographiccitation.journal","Autophagy"],["dc.bibliographiccitation.lastpage","1550"],["dc.bibliographiccitation.volume","7"],["dc.contributor.author","Nair, Usha"],["dc.contributor.author","Thumm, Michael"],["dc.contributor.author","Klionsky, Daniel J."],["dc.contributor.author","Krick, Roswitha"],["dc.date.accessioned","2018-11-07T08:49:08Z"],["dc.date.available","2018-11-07T08:49:08Z"],["dc.date.issued","2011"],["dc.description.abstract","Perhaps the most complex step of macroautophagy is the formation of the double-membrane autophagosome. The majority of the autophagy-related (Atg) proteins are thought to participate in nucleation and expansion of the phagophore, and/or the completion of this compartment. Monitoring this part of the process is difficult, and typically involves electron microscopy analysis; however, unless three-dimensional tomography is performed, even this method cannot be used to easily determine if the phagophore is completely enclosed. Accordingly, a complementary approach is to examine the accessibility of sequestered cargo to exogenausly added protease. This type of protease protection analysis has been used to monitor the formation of cytoplasm-to-vacuole targeting (Cvt) vesicles and autophagosomes by examining the protease sensitivity of precursor aminopeptidase I (prApe1). For determining the status of autophagosomes formed during nonselective autophagy, however, prApe1 is not the best marker protein. Here, we describe an alternative method for examining autophagosome completion using GFP-Atg8 as a marker for protease protection."],["dc.description.sponsorship","National Institutes of Health [GM53396]; Deutsche Forschungsgemeinschaft"],["dc.identifier.doi","10.4161/auto.7.12.18424"],["dc.identifier.isi","000298182600013"],["dc.identifier.pmid","22108003"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/21384"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Landes Bioscience"],["dc.relation.issn","1554-8627"],["dc.title","GFP-Atg8 protease protection as a tool to monitor autophagosome biogenesis"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","896"],["dc.bibliographiccitation.issue","7"],["dc.bibliographiccitation.journal","Autophagy"],["dc.bibliographiccitation.lastpage","910"],["dc.bibliographiccitation.volume","4"],["dc.contributor.author","Krick, Roswitha"],["dc.contributor.author","Henke, Sandra"],["dc.contributor.author","Tolstrup, Joern"],["dc.contributor.author","Thumm, Michael"],["dc.date.accessioned","2021-06-01T10:48:54Z"],["dc.date.available","2021-06-01T10:48:54Z"],["dc.date.issued","2008"],["dc.description.abstract","Atg18p and Atg21p are two highly homologous yeast autophagy proteins. Atg18p functions in both autophagy and the selective Cvt-pathway, while the function of Atg21p is restricted to the Cvt-pathway. The yeast genome encodes with Ygr223cp (Hsv2p), a third member of this protein family. So far no function has been assigned to Ygr223cp. By colocalization with the endosomal marker Snf7-RFP and an RFP-tagged FYVE domain, we here identify the localization of a pool of Atg18p, Atg21p and Ygr223cp at endosomes. Endosomal recruitment of all three proteins depends on PtdIns3P generated by the Vps34-complex II containing Vps38p, but not on the function of the Vps34-complex I. Since only the Vps34-complex I is essential for autophagy, we expect that at endosomes Atg18p, Atg21p and Ygr223cp have a function distinct from autophagy. Some Vps Class D mutants involved in Golgi-to-endosome transport are required for the endosomal recruitment of GFP-Atg18p, -Atg21p and -Ygr223cp. These include the Qa-SNARE Pep12p, its SM protein Vps45p, the Rab GTPase Vps21p and the Rab effector Vac1p. Deletion of ATG18, ATG21 and YGR223c, alone or simultaneously has no obvious function on the MVB-pathway and CPY-sorting. However, overexpression of ATG21 leads to CPY secretion. We further show, to our knowledge for the first time, that Ygr223cp affects an autophagic process, namely micronucleophagy."],["dc.identifier.doi","10.4161/auto.6801"],["dc.identifier.isi","000259829700007"],["dc.identifier.pmid","18769150"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/86096"],["dc.language.iso","en"],["dc.notes.intern","DOI-Import GROB-425"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Taylor & Francis Inc"],["dc.relation.eissn","1554-8635"],["dc.relation.issn","1554-8627"],["dc.title","Dissecting the localization and function of Atg18, Atg21 and Ygr223c"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","965"],["dc.bibliographiccitation.issue","6"],["dc.bibliographiccitation.journal","The Journal of Cell Biology"],["dc.bibliographiccitation.lastpage","973"],["dc.bibliographiccitation.volume","190"],["dc.contributor.author","Krick, Roswitha"],["dc.contributor.author","Bremer, Sebastian"],["dc.contributor.author","Welter, Evelyn"],["dc.contributor.author","Schlotterhose, Petra"],["dc.contributor.author","Muehe, Yvonne"],["dc.contributor.author","Eskelinen, Eeva-Liisa"],["dc.contributor.author","Thumm, Michael"],["dc.date.accessioned","2018-11-07T08:39:07Z"],["dc.date.available","2018-11-07T08:39:07Z"],["dc.date.issued","2010"],["dc.description.abstract","The molecular details of the biogenesis of double-membraned autophagosomes are poorly understood. We identify the Saccharomyces cerevisiae AAA-adenosine triphosphatase Cdc48 and its substrate-recruiting cofactor Shp1/Ubx1 as novel components needed for autophagosome biogenesis. In mammals, the Cdc48 homologue p97/VCP and the Shp1 homologue p47 mediate Golgi reassembly by extracting an unknown mono-ubiquitinated fusion regulator from a complex. We find no requirement of ubiquitination or the proteasome system for autophagosome biogenesis but detect interaction of Shp1 with the ubiquitin-fold autophagy protein Atg8. Atg8 coupled to phosphatidylethanolamine ( PE) is crucial for autophagosome elongation and, in vitro, mediates tethering and hemifusion. Interaction with Shp1 requires an FK motif within the N-terminal non-ubiquitin-like Atg8 domain. Based on our data, we speculate that autophagosome formation, in contrast to Golgi reassembly, requires a complex in which Atg8 functionally substitutes ubiquitin. This, for the first time, would give a rationale for use of the ubiquitin-like Atg8 during macroautophagy and would explain why Atg8-PE delipidation is necessary for efficient macroautophagy."],["dc.description.sponsorship","Deutsche Forschungsgemeinschaft"],["dc.identifier.doi","10.1083/jcb.201002075"],["dc.identifier.isi","000282604600005"],["dc.identifier.pmid","20855502"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/6296"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/18915"],["dc.notes.intern","Merged from goescholar"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Rockefeller Univ Press"],["dc.relation.issn","0021-9525"],["dc.rights","Goescholar"],["dc.rights.uri","https://goescholar.uni-goettingen.de/licenses"],["dc.title","Cdc48/p97 and Shp1/p47 regulate autophagosome biogenesis in concert with ubiquitin-like Atg8"],["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","4492"],["dc.bibliographiccitation.issue","10"],["dc.bibliographiccitation.journal","Molecular Biology of the Cell"],["dc.bibliographiccitation.lastpage","4505"],["dc.bibliographiccitation.volume","19"],["dc.contributor.author","Krick, Roswitha"],["dc.contributor.author","Muehe, Yvonne"],["dc.contributor.author","Prick, Tanja"],["dc.contributor.author","Bremer, S."],["dc.contributor.author","Schlotterhose, Petra"],["dc.contributor.author","Eskelinen, E-L."],["dc.contributor.author","Millen, Jonathan I."],["dc.contributor.author","Goldfarb, David S."],["dc.contributor.author","Thumm, Michael"],["dc.date.accessioned","2018-11-07T11:10:42Z"],["dc.date.available","2018-11-07T11:10:42Z"],["dc.date.issued","2008"],["dc.description.abstract","Autophagy is a diverse family of processes that transport cytoplasm and organelles into the lysosome/vacuole lumen for degradation. During macroautophagy cargo is packaged in autophagosomes that fuse with the lysosome/vacuole. During microautophagy cargo is directly engulfed by the lysosome/vacuole membrane. Piecemeal microautophagy of the nucleus (PMN) occurs in Saccharomyces cerevisiae at nucleus-vacuole (NV) junctions and results in the pinching-off and release into the vacuole of nonessential portions of the nucleus. Previous studies concluded macroautophagy ATG genes are not absolutely required for PMN. Here we report using two biochemical assays that PMN is efficiently inhibited in atg mutant cells: PMN blebs are produced, but vesicles are rarely released into the vacuole lumen. Electron microscopy of arrested PMN structures in atg7, atg8, and atg9 mutant cells suggests that NV-junction-associated micronuclei may normally be released from the nucleus before their complete enclosure by the vacuole membrane. In this regard PMN is similar to the microautophagy of peroxisomes (micropexophagy), where the side of the peroxisome opposite the engulfing vacuole is capped by a structure called the \"micropexophagy-specific membrane apparatus\" (MIPA). The MIPA contains Atg proteins and facilitates terminal enclosure and fusion steps. PMN does not require the complete vacuole homotypic fusion genes. We conclude that a spectrum of ATG genes is required for the terminal vacuole enclosure and fusion stages of PMN."],["dc.description.sponsorship","National Science Foundation [MCB-072064]"],["dc.identifier.doi","10.1091/mbc.E08-04-0363"],["dc.identifier.isi","000260472200042"],["dc.identifier.pmid","18701704"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/53267"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Amer Soc Cell Biology"],["dc.relation.issn","1059-1524"],["dc.title","Piecemeal Microautophagy of the Nucleus Requires the Core Macroautophagy Genes"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.journal","Yeast"],["dc.bibliographiccitation.volume","30"],["dc.contributor.author","Krick, Roswitha"],["dc.contributor.author","Busse, Ricarda A."],["dc.contributor.author","Thumm, Michael"],["dc.contributor.author","Kuehnel, Karin"],["dc.date.accessioned","2018-11-07T09:20:10Z"],["dc.date.available","2018-11-07T09:20:10Z"],["dc.date.issued","2013"],["dc.format.extent","36"],["dc.identifier.isi","000327927400028"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/28818"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Wiley-blackwell"],["dc.publisher.place","Hoboken"],["dc.relation.conference","26th International Conference on Yeast Genetics and Molecular Biology"],["dc.relation.eventlocation","Frankfurt Main, GERMANY"],["dc.relation.issn","1097-0061"],["dc.relation.issn","0749-503X"],["dc.title","PROPPINs in autophagy"],["dc.type","conference_abstract"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","955"],["dc.bibliographiccitation.issue","7"],["dc.bibliographiccitation.journal","The EMBO Journal"],["dc.bibliographiccitation.lastpage","973"],["dc.bibliographiccitation.volume","34"],["dc.contributor.author","Juris, Lisa"],["dc.contributor.author","Montino, Marco"],["dc.contributor.author","Rube, Peter"],["dc.contributor.author","Schlotterhose, Petra"],["dc.contributor.author","Thumm, Michael"],["dc.contributor.author","Krick, Roswitha"],["dc.date.accessioned","2018-11-07T09:59:04Z"],["dc.date.available","2018-11-07T09:59:04Z"],["dc.date.issued","2015"],["dc.description.abstract","Autophagosome biogenesis requires two ubiquitin-like conjugation systems. One couples ubiquitin-like Atg8 to phosphatidylethanolamine, and the other couples ubiquitin-like Atg12 to Atg5. Atg12 similar to Atg5 then forms a heterodimer with Atg16. Membrane recruitment of the Atg12 similar to Atg5/Atg16 complex defines the Atg8 lipidation site. Lipidation requires a PI3P-containing precursor. How PI3P is sensed and used to coordinate the conjugation systems remained unclear. Here, we show that Atg21, a WD40 beta-propeller, binds via PI3P to the preautophagosomal structure (PAS). Atg21 directly interacts with the coiled-coil domain of Atg16 and with Atg8. This latter interaction requires the conserved F5K6-motif in the N-terminal helical domain of Atg8, but not its AIM-binding site. Accordingly, the Atg8 AIM-binding site remains free to mediate interaction with its E2 enzyme Atg3. Atg21 thus defines PI3P-dependently the lipidation site by linking and organising the E3 ligase complex and Atg8 at the PAS."],["dc.identifier.doi","10.15252/embj.201488957"],["dc.identifier.isi","000352167300012"],["dc.identifier.pmid","25691244"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/37507"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Wiley-blackwell"],["dc.relation.issn","1460-2075"],["dc.relation.issn","0261-4189"],["dc.title","PI3P binding by Atg21 organises Atg8 lipidation"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.issue","6"],["dc.bibliographiccitation.journal","Autophagy"],["dc.bibliographiccitation.volume","5"],["dc.contributor.author","Thumm, Michael"],["dc.contributor.author","Bremer, Sebastian"],["dc.contributor.author","Welter, Evelyn"],["dc.contributor.author","Eskelinen, Eeva-Liisa"],["dc.contributor.author","Krick, Roswitha"],["dc.date.accessioned","2018-11-07T11:25:41Z"],["dc.date.available","2018-11-07T11:25:41Z"],["dc.date.issued","2009"],["dc.format.extent","897"],["dc.identifier.isi","000269021700039"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/56684"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Landes Bioscience"],["dc.publisher.place","Austin"],["dc.relation.issn","1554-8627"],["dc.title","Molecular mechanism of micronucleophagy (piecemeal microautophagy of the nucleus, PMN) in S. cerevisiae"],["dc.type","conference_abstract"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","4970"],["dc.bibliographiccitation.issue","20"],["dc.bibliographiccitation.journal","FEBS Journal"],["dc.bibliographiccitation.lastpage","4982"],["dc.bibliographiccitation.volume","280"],["dc.contributor.author","Welter, Evelyn"],["dc.contributor.author","Montino, Marco"],["dc.contributor.author","Reinhold, Robert"],["dc.contributor.author","Schlotterhose, Petra"],["dc.contributor.author","Krick, Roswitha"],["dc.contributor.author","Dudek, Jan"],["dc.contributor.author","Rehling, Peter"],["dc.contributor.author","Thumm, Michael"],["dc.date.accessioned","2017-09-07T11:47:07Z"],["dc.date.available","2017-09-07T11:47:07Z"],["dc.date.issued","2013"],["dc.description.abstract","Mitochondria are turned over by an autophagic process termed mitophagy. This process is considered to remove damaged, superfluous and aged organelles. However, little is known about how defective organelles are recognized, what types of damage induce turnover, and whether an identical set of factors contributes to degradation under different conditions. Here we systematically compared the mitophagy rate and requirement for mitophagy-specific proteins during post-log-phase and rapamycin-induced mitophagy. To specifically assess mitophagy of damaged mitochondria, we analyzed cells accumulating proteins prone to degradation due to lack of the mitochondrial AAA-protease Yme1. While autophagy 32 (Atg32) was required under all tested conditions, the function of Atg33 could be partially bypassed in post-log-phase and rapamycin-induced mitophagy. Unexpectedly, we found that Uth1 was dispensable for mitophagy. A re-evaluation of its mitochondrial localization revealed that Uth1 is a protein of the inner mitochondrial membrane that is targeted by a cleavable N-terminal pre-sequence. In agreement with our functional analyses, this finding excludes a role of Uth1 as a mitochondrial surface receptor."],["dc.identifier.doi","10.1111/febs.12468"],["dc.identifier.gro","3142274"],["dc.identifier.isi","000327132100006"],["dc.identifier.pmid","23910823"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/6465"],["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","1742-4658"],["dc.relation.issn","1742-464X"],["dc.title","Uth1 is a mitochondrial inner membrane protein dispensable for post-log-phase and rapamycin-induced mitophagy"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dspace.entity.type","Publication"]]