Kilisch, Markus

[["dc.bibliographiccitation.firstpage","eaaz1436"],["dc.bibliographiccitation.issue","647"],["dc.bibliographiccitation.journal","Science Signaling"],["dc.bibliographiccitation.volume","13"],["dc.contributor.author","Menzel, Julia"],["dc.contributor.author","Kownatzki-Danger, Daniel"],["dc.contributor.author","Tokar, Sergiy"],["dc.contributor.author","Ballone, Alice"],["dc.contributor.author","Unthan-Fechner, Kirsten"],["dc.contributor.author","Kilisch, Markus"],["dc.contributor.author","Lenz, Christof"],["dc.contributor.author","Urlaub, Henning"],["dc.contributor.author","Mori, Mattia"],["dc.contributor.author","Ottmann, Christian"],["dc.contributor.author","Shattock, Michael J."],["dc.contributor.author","Lehnart, Stephan E."],["dc.contributor.author","Schwappach, Blanche"],["dc.date.accessioned","2021-04-14T08:32:51Z"],["dc.date.available","2021-04-14T08:32:51Z"],["dc.date.issued","2020"],["dc.identifier.doi","10.1126/scisignal.aaz1436"],["dc.identifier.pmid","32873725"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/84038"],["dc.identifier.url","https://mbexc.uni-goettingen.de/literature/publications/68"],["dc.identifier.url","https://sfb1002.med.uni-goettingen.de/production/literature/publications/368"],["dc.identifier.url","https://sfb1190.med.uni-goettingen.de/production/literature/publications/126"],["dc.language.iso","en"],["dc.notes.intern","DOI Import GROB-399"],["dc.relation","EXC 2067: Multiscale Bioimaging"],["dc.relation","SFB 1002: Modulatorische Einheiten bei Herzinsuffizienz"],["dc.relation","SFB 1002 | A07: Rolle der TRC40-Maschinerie im Proteostase-Netzwerk von Kardiomyozyten"],["dc.relation","SFB 1190: Transportmaschinen und Kontaktstellen zellulärer Kompartimente"],["dc.relation.eissn","1937-9145"],["dc.relation.issn","1945-0877"],["dc.relation.workinggroup","RG Lehnart"],["dc.relation.workinggroup","RG Schwappach (Membrane Protein Biogenesis)"],["dc.relation.workinggroup","RG Lenz"],["dc.relation.workinggroup","RG Urlaub (Bioanalytische Massenspektrometrie)"],["dc.title","14-3-3 binding creates a memory of kinase action by stabilizing the modified state of phospholamban"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.subtype","original_ja"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","269"],["dc.bibliographiccitation.issue","2"],["dc.bibliographiccitation.journal","Biomolecules"],["dc.bibliographiccitation.volume","11"],["dc.contributor.author","Kilisch, Markus"],["dc.contributor.author","Götzke, Hansjörg"],["dc.contributor.author","Gere-Becker, Maja"],["dc.contributor.author","Crauel, Alexander"],["dc.contributor.author","Opazo, Felipe"],["dc.contributor.author","Frey, Steffen"],["dc.date.accessioned","2021-04-14T08:29:47Z"],["dc.date.available","2021-04-14T08:29:47Z"],["dc.date.issued","2021"],["dc.identifier.doi","10.3390/biom11020269"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/82990"],["dc.language.iso","en"],["dc.notes.intern","DOI Import GROB-399"],["dc.relation.eissn","2218-273X"],["dc.title","Discovery and Characterization of an ALFA-Tag-Specific Affinity Resin Optimized for Protein Purification at Low Temperatures in Physiological Buffer"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","jcs232835"],["dc.bibliographiccitation.issue","2"],["dc.bibliographiccitation.journal","Journal of Cell Science"],["dc.bibliographiccitation.volume","133"],["dc.contributor.author","Kilisch, Markus"],["dc.contributor.author","Mayer, Simone"],["dc.contributor.author","Mitkovski, Miso"],["dc.contributor.author","Roehse, Heiko"],["dc.contributor.author","Hentrich, Jennifer"],["dc.contributor.author","Schwappach, Blanche"],["dc.contributor.author","Papadopoulos, Theofilos"],["dc.date.accessioned","2020-12-10T18:41:54Z"],["dc.date.available","2020-12-10T18:41:54Z"],["dc.date.issued","2020"],["dc.identifier.doi","10.1242/jcs.232835"],["dc.identifier.eissn","1477-9137"],["dc.identifier.issn","0021-9533"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/77720"],["dc.language.iso","en"],["dc.notes.intern","DOI Import GROB-354"],["dc.title","A GTPase-induced switch in phospholipid affinity of collybistin contributes to synaptic gephyrin clustering"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["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","886"],["dc.bibliographiccitation.issue","6"],["dc.bibliographiccitation.journal","EMBO Journal"],["dc.bibliographiccitation.lastpage","898"],["dc.bibliographiccitation.volume","32"],["dc.contributor.author","Lytovchenko, Oleksandr"],["dc.contributor.author","Melin, Jonathan"],["dc.contributor.author","Schulz, Christian"],["dc.contributor.author","Kilisch, Markus"],["dc.contributor.author","Hutu, Dana P."],["dc.contributor.author","Rehling, Peter"],["dc.date.accessioned","2017-09-07T11:47:45Z"],["dc.date.available","2017-09-07T11:47:45Z"],["dc.date.issued","2013"],["dc.description.abstract","The mitochondrial presequence translocase interacts with presequence-containing precursors at the intermembrane space (IMS) side of the inner membrane to mediate their translocation into the matrix. Little is known as too how these matrix-targeting signals activate the translocase in order to initiate precursor transport. Therefore, we analysed how signal recognition by the presequence translocase initiates reorganization among Tim-proteins during import. Our analyses revealed that the presequence receptor Tim50 interacts with Tim21 in a signal-sensitive manner in a process that involves the IMS-domain of the Tim23 channel. The signal-driven release of Tim21 from Tim50 promotes recruitment of Pam17 and thus triggers formation of the motor-associated form of the TIM23 complex required for matrix transport. The EMBO Journal (2013) 32, 886-898. doi:10.1038/emboj.2013.23; Published online 12 February 2013"],["dc.identifier.doi","10.1038/emboj.2013.23"],["dc.identifier.gro","3142372"],["dc.identifier.isi","000316463600013"],["dc.identifier.pmid","23403928"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/7552"],["dc.language.iso","en"],["dc.notes.intern","WoS Import 2017-03-10"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.relation.issn","0261-4189"],["dc.title","Signal recognition initiates reorganization of the presequence translocase during protein import"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","32787"],["dc.bibliographiccitation.issue","45"],["dc.bibliographiccitation.journal","Journal of Biological Chemistry"],["dc.bibliographiccitation.lastpage","32796"],["dc.bibliographiccitation.volume","288"],["dc.contributor.author","Pilla, Esther"],["dc.contributor.author","Kilisch, Markus"],["dc.contributor.author","Lenz, Christof"],["dc.contributor.author","Urlaub, Henning"],["dc.contributor.author","Geiss-Friedlander, Ruth"],["dc.date.accessioned","2018-11-07T09:17:38Z"],["dc.date.available","2018-11-07T09:17:38Z"],["dc.date.issued","2013"],["dc.description.abstract","Background: SUMO1 binds to an arm motif in the prolyl-peptidase DPP9, leading to allosteric activation of the peptidase. Results: A SUMO1 peptide covering the DPP9 interaction surface inhibits DPP9 activity. Inhibition is dependent on residues in the DPP9 arm motif. Conclusion: The SUMO1 peptide and its variants are allosteric DPP9 inhibitors. Significance: This work highlights the potential use of peptides mimicking interaction surfaces for modulating enzyme activity. The intracellular peptidases dipeptidyl peptidase (DPP) 8 and DPP9 are involved in multiple cellular pathways including antigen maturation, cellular homeostasis, energy metabolism, and cell viability. Previously we showed that the small ubiquitin-like protein modifier SUMO1 interacts with an armlike structure in DPP9, leading to allosteric activation of the peptidase. Here we demonstrate that the E67-interacting loop (EIL) peptide, which corresponds to the interaction surface of SUMO1 with DPP9, acts as a noncompetitive inhibitor of DPP9. Moreover, by analyzing the sensitivity of DPP9 arm mutants to the EIL peptide, we mapped specific residues in the arm that are important for inhibition by the EIL, suggesting that the peptide acts as an allosteric inhibitor of DPP9. By modifying the EIL peptide, we constructed peptide variants with more than a 1,000-fold selectivity toward DPP8 (147 nm) and DPP9 (170 nm) over DPPIV (200 m). Furthermore, application of these peptides to cells leads to a clear inhibition of cellular prolyl peptidase activity. Importantly, in line with previous publications, inhibition of DPP9 with these novel allosteric peptide inhibitors leads to an increase in EGF-mediated phosphorylation of Akt. This work highlights the potential use of peptides that mimic interaction surfaces for modulating enzyme activity."],["dc.description.sponsorship","Deutsche Forschungsgemeinschaft [2234/1-1, 1086/2]"],["dc.identifier.doi","10.1074/jbc.M113.489179"],["dc.identifier.isi","000328681700062"],["dc.identifier.pmid","24072711"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/28214"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Amer Soc Biochemistry Molecular Biology Inc"],["dc.relation.issn","1083-351X"],["dc.relation.issn","0021-9258"],["dc.title","The SUMO1-E67 Interacting Loop Peptide Is an Allosteric Inhibitor of the Dipeptidyl Peptidases 8 and 9"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","1105"],["dc.bibliographiccitation.issue","5"],["dc.bibliographiccitation.journal","Pflügers Archiv European Journal of Physiology"],["dc.bibliographiccitation.lastpage","1120"],["dc.bibliographiccitation.volume","467"],["dc.contributor.author","Kilisch, Markus"],["dc.contributor.author","Lytovchenko, Olga"],["dc.contributor.author","Schwappach, Blanche"],["dc.contributor.author","Renigunta, Vijay"],["dc.contributor.author","Daut, Jürgen"],["dc.date.accessioned","2017-09-07T11:44:25Z"],["dc.date.available","2017-09-07T11:44:25Z"],["dc.date.issued","2015"],["dc.description.abstract","The intracellular transport of membrane proteins is controlled by trafficking signals: Short peptide motifs that mediate the contact with COPI, COPII or various clathrin-associated coat proteins. In addition, many membrane proteins interact with accessory proteins that are involved in the sorting of these proteins to different intracellular compartments. In the K-2P channels, TASK-1 and TASK-3, the influence of protein-protein interactions on sorting decisions has been studied in some detail. Both TASK paralogues interact with the adaptor protein 14-3-3; TASK-1 interacts, in addition, with the adaptor protein p11 (S100A10) and the endosomal SNARE protein syntaxin-8. The role of these interacting proteins in controlling the intracellular traffic of the channels and the underlying molecular mechanisms are summarised in this review. In the case of 14-3-3, the interacting protein masks a retention signal in the C-terminus of the channel; in the case of p11, the interacting protein carries a retention signal that localises the channel to the endoplasmic reticulum; and in the case of syntaxin-8, the interacting protein carries an endocytosis signal that complements an endocytosis signal of the channel. These examples illustrate some of the mechanisms by which interacting proteins may determine the itinerary of a membrane protein within a cell and suggest that the intracellular traffic of membrane proteins may be adapted to the specific functions of that protein by multiple protein-protein interactions."],["dc.identifier.doi","10.1007/s00424-014-1672-2"],["dc.identifier.gro","3141914"],["dc.identifier.isi","000352847000019"],["dc.identifier.pmid","25559843"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/2478"],["dc.notes.intern","WoS Import 2017-03-10 / Funder: Deutsche Forschungsgemeinschaft [FOR 1086, TP7, TP9, SFB 593, TP4]"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.publisher","Springer"],["dc.relation.eissn","1432-2013"],["dc.relation.issn","0031-6768"],["dc.title","The role of protein-protein interactions in the intracellular traffic of the potassium channels TASK-1 and TASK-3"],["dc.type","review"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dspace.entity.type","Publication"]]