Thoms, Sven

[["dc.bibliographiccitation.firstpage","504"],["dc.bibliographiccitation.issue","3"],["dc.bibliographiccitation.journal","The FEBS Journal"],["dc.bibliographiccitation.lastpage","514"],["dc.bibliographiccitation.volume","275"],["dc.contributor.author","Thoms, Sven"],["dc.contributor.author","Debelyy, Mykhaylo O."],["dc.contributor.author","Nau, Katja"],["dc.contributor.author","Meyer, Helmut E."],["dc.contributor.author","Erdmann, Ralf"],["dc.date.accessioned","2020-08-10T05:24:04Z"],["dc.date.available","2020-08-10T05:24:04Z"],["dc.date.issued","2008"],["dc.description.abstract","Lpx1p (systematic name: Yor084wp) is a peroxisomal protein from Saccharomyces cerevisiae with a peroxisomal targeting signal type 1 (PTS1) and a lipase motif. Using mass spectrometry, we have identified Lpx1p as present in peroxisomes, and show that Lpx1p import is dependent on the PTS1 receptor Pex5p. We provide evidence that Lpx1p is piggyback-transported into peroxisomes. We have expressed the Lpx1p protein in Escherichia coli, and show that the enzyme exerts acyl hydrolase and phospholipase A activity in vitro. However, the protein is not required for wild-type-like steady-state function of peroxisomes, which might be indicative of a metabolic rather than a biogenetic role. Interestingly, peroxisomes in deletion mutants of LPX1 have an aberrant morphology characterized by intraperoxisomal vesicles or invaginations."],["dc.identifier.doi","10.1111/j.1742-4658.2007.06217.x"],["dc.identifier.pmid","18199283"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/67542"],["dc.language.iso","en"],["dc.relation.issn","1742-464X"],["dc.title","Lpx1p is a peroxisomal lipase required for normal peroxisome morphology"],["dc.type","journal_article"],["dc.type.internalPublication","no"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","541"],["dc.bibliographiccitation.lastpage","572"],["dc.contributor.author","Platta, Harald W."],["dc.contributor.author","Thoms, Sven"],["dc.contributor.author","Kunau, Wolf‐H."],["dc.contributor.author","Erdmann, Ralf"],["dc.contributor.editor","Dalbey, Ross E."],["dc.contributor.editor","Koehler, Carla M."],["dc.contributor.editor","Tamanoi, Fuyuhiko"],["dc.date.accessioned","2020-08-10T06:04:52Z"],["dc.date.available","2020-08-10T06:04:52Z"],["dc.date.issued","2007"],["dc.description.abstract","This chapter discusses the enzymatically catalyzed mechanisms underlying the transport of matrix proteins across the peroxisomal membrane into the lumen of the organelle, a process that involves most of the known peroxins. The chapter focuses on the basic experimental evidence concerning the functional roles of Pex4p and AAA peroxins in Pex5p recycling and matrix protein import to combine and discuss them in a unified model. Ubiquitin-conjugating enzymes play a central role in the process of ubiquitination and function to bridge the first, nonspecific step of ubiquitin activation by E1 with the transfer of activated ubiquitin to target-proteins by substrate-specific E3 enzymes. Pex4p/Ubc10p is a ubiquitin-conjugating enzyme essential for peroxisomal biogenesis. Pex4p contains the catalytically relevant active site Cys residue of ubiquitin-conjugating enzymes within the core Ubc fold, while AAAs are mechanoenzymes that manipulate the structure of substrate proteins, and thereby unfold them or disassemble protein complexes. The energy dependence of peroxisomal protein import is caused by the cycle of the peroxisomal targeting signal (PTS) receptors. A model is emerging in which the previously disparate roles of Pex4p and the AAA peroxins are combined in a concerted reaction sequence. However, it will be a challenge to elucidate the way ATP-dependent receptor dislocation is mechanistically linked to the import of folded proteins."],["dc.identifier.doi","10.1016/S1874-6047(07)25021-8"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/67555"],["dc.language.iso","en"],["dc.publisher","Elsevier"],["dc.relation.isbn","9780123739162"],["dc.relation.ispartof","Molecular Machines Involved in Protein Transport across Cellular Membranes"],["dc.title","Function of the Ubiquitin‐Conjugating Enzyme Pex4p and the AAA Peroxin Complex Pex1p/Pex6p in Peroxisomal Matrix Protein Transport"],["dc.type","book_chapter"],["dc.type.internalPublication","no"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","947"],["dc.bibliographiccitation.issue","7"],["dc.bibliographiccitation.journal","Traffic"],["dc.bibliographiccitation.lastpage","959"],["dc.bibliographiccitation.volume","13"],["dc.contributor.author","Otzen, Marleen"],["dc.contributor.author","Rucktäschel, Robert"],["dc.contributor.author","Thoms, Sven"],["dc.contributor.author","Emmrich, Kerstin"],["dc.contributor.author","Krikken, Arjen M."],["dc.contributor.author","Erdmann, Ralf"],["dc.contributor.author","van der Klei, Ida J."],["dc.date.accessioned","2020-08-10T05:14:16Z"],["dc.date.available","2020-08-10T05:14:16Z"],["dc.date.issued","2012"],["dc.description.abstract","During budding of yeast cells peroxisomes are distributed over mother cell and bud, a process that involves the myosin motor protein Myo2p and the peroxisomal membrane protein Inp2p. Here, we show that Pex19p, a peroxin implicated in targeting and complex formation of peroxisomal membrane proteins, also plays a role in peroxisome partitioning. Binding studies revealed that Pex19p interacts with the cargo-binding domain of Myo2p. We identified mutations in Myo2p that specifically reduced binding to Pex19p, but not to Inp2p. The interaction between Myo2p and Pex19p was also reduced by a mutation that blocked Pex19p farnesylation. Microscopy revealed that the Pex19p-Myo2p interaction is important for peroxisome inheritance, because mutations that affect this interaction hamper peroxisome inheritance in vivo. Together these data suggest that both Inp2p and Pex19p are required for proper association of peroxisomes to Myo2p."],["dc.identifier.doi","10.1111/j.1600-0854.2012.01364.x"],["dc.identifier.pmid","22486971"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/67537"],["dc.language.iso","en"],["dc.relation.eissn","1600-0854"],["dc.relation.issn","1398-9219"],["dc.title","Pex19p contributes to peroxisome inheritance in the association of peroxisomes to Myo2p"],["dc.type","journal_article"],["dc.type.internalPublication","no"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","5169"],["dc.bibliographiccitation.issue","20"],["dc.bibliographiccitation.journal","The FEBS Journal"],["dc.bibliographiccitation.lastpage","5181"],["dc.bibliographiccitation.volume","272"],["dc.contributor.author","Thoms, Sven"],["dc.contributor.author","Erdmann, Ralf"],["dc.date.accessioned","2020-08-10T05:27:04Z"],["dc.date.available","2020-08-10T05:27:04Z"],["dc.date.issued","2005"],["dc.description.abstract","The abundance and size of cellular organelles vary depending on the cell type and metabolic needs. Peroxisomes constitute a class of cellular organelles renowned for their ability to adapt to cellular and environmental conditions. Together with transcriptional regulators, two groups of peroxisomal proteins have a pronounced influence on peroxisome size and abundance. Pex11-type peroxisome proliferators are involved in the proliferation of peroxisomes, defined here as an increase in size and/or number of peroxisomes. Dynamin-related proteins have recently been suggested to be required for the scission of peroxisomal membranes. This review surveys the function of Pex11-type peroxisome proliferators and dynamin-related proteins in peroxisomal proliferation and division."],["dc.identifier.doi","10.1111/j.1742-4658.2005.04939.x"],["dc.identifier.pmid","16218949"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/67544"],["dc.language.iso","en"],["dc.relation.issn","1742-464X"],["dc.title","Dynamin-related proteins and Pex11 proteins in peroxisome division and proliferation"],["dc.type","journal_article"],["dc.type.internalPublication","no"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","770"],["dc.bibliographiccitation.issue","6"],["dc.bibliographiccitation.journal","Eukaryotic Cell"],["dc.bibliographiccitation.lastpage","775"],["dc.bibliographiccitation.volume","10"],["dc.contributor.author","Thoms, Sven"],["dc.contributor.author","Debelyy, Mykhaylo O."],["dc.contributor.author","Connerth, Melanie"],["dc.contributor.author","Daum, Günther"],["dc.contributor.author","Erdmann, Ralf"],["dc.date.accessioned","2020-08-10T05:59:18Z"],["dc.date.available","2020-08-10T05:59:18Z"],["dc.date.issued","2011"],["dc.description.abstract","Here, we report the identification of a novel hydrolase in Saccharomyces cerevisiae. Ldh1p (systematic name, Ybr204cp) comprises the typical GXSXG-type lipase motif of members of the α/β-hydrolase family and shares some features with the peroxisomal lipase Lpx1p. Both proteins carry a putative peroxisomal targeting signal type1 (PTS1) and can be aligned with two regions of homology. While Lpx1p is known as a peroxisomal enzyme, subcellular localization studies revealed that Ldh1p is predominantly localized to lipid droplets, the storage compartment of nonpolar lipids. Ldh1p is not required for the function and biogenesis of peroxisomes, and targeting of Ldh1p to lipid droplets occurs independently of the PTS1 receptor Pex5p."],["dc.identifier.doi","10.1128/EC.05038-11"],["dc.identifier.pmid","21478430"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/67554"],["dc.language.iso","en"],["dc.relation.eissn","1535-9786"],["dc.relation.issn","1535-9778"],["dc.title","The putative Saccharomyces cerevisiae hydrolase Ldh1p is localized to lipid droplets"],["dc.type","journal_article"],["dc.type.internalPublication","unknown"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","20885"],["dc.bibliographiccitation.issue","31"],["dc.bibliographiccitation.journal","The Journal of Biological Chemistry"],["dc.bibliographiccitation.lastpage","20896"],["dc.bibliographiccitation.volume","284"],["dc.contributor.author","Rucktäschel, Robert"],["dc.contributor.author","Thoms, Sven"],["dc.contributor.author","Sidorovitch, Vadim"],["dc.contributor.author","Halbach, Andre"],["dc.contributor.author","Pechlivanis, Markos"],["dc.contributor.author","Volkmer, Rudolf"],["dc.contributor.author","Alexandrov, Kirill"],["dc.contributor.author","Kuhlmann, Jürgen"],["dc.contributor.author","Rottensteiner, Hanspeter"],["dc.contributor.author","Erdmann, Ralf"],["dc.date.accessioned","2020-08-10T05:20:25Z"],["dc.date.available","2020-08-10T05:20:25Z"],["dc.date.issued","2009"],["dc.description.abstract","The conserved CaaX box peroxin Pex19p is known to be modified by farnesylation. The possible involvement of this lipid modification in peroxisome biogenesis, the degree to which Pex19p is farnesylated, and its molecular function are unknown or controversial. We resolve these issues by first showing that the complete pool of Pex19p is processed by farnesyltransferase in vivo and that this modification is independent of peroxisome induction or the Pex19p membrane anchor Pex3p. Furthermore, genomic mutations of PEX19 prove that farnesylation is essential for proper matrix protein import into peroxisomes, which is supposed to be caused indirectly by a defect in peroxisomal membrane protein (PMP) targeting or stability. This assumption is corroborated by the observation that mutants defective in Pex19p farnesylation are characterized by a significantly reduced steady-state concentration of prominent PMPs (Pex11p, Ant1p) but also of essential components of the peroxisomal import machinery, especially the RING peroxins, which were almost depleted from the importomer. In vivo and in vitro, PMP recognition is only efficient when Pex19p is farnesylated with affinities differing by a factor of 10 between the non-modified and wild-type forms of Pex19p. Farnesylation is likely to induce a conformational change in Pex19p. Thus, isoprenylation of Pex19p contributes to substrate membrane protein recognition for the topogenesis of PMPs, and our results highlight the importance of lipid modifications in protein-protein interactions."],["dc.identifier.doi","10.1074/jbc.M109.016584"],["dc.identifier.pmid","19451657"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/67540"],["dc.language.iso","en"],["dc.relation.eissn","1083-351X"],["dc.relation.issn","0021-9258"],["dc.title","Farnesylation of pex19p is required for its structural integrity and function in peroxisome biogenesis"],["dc.type","journal_article"],["dc.type.internalPublication","no"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","1620"],["dc.bibliographiccitation.issue","12"],["dc.bibliographiccitation.journal","Biochimica et Biophysica Acta"],["dc.bibliographiccitation.lastpage","1628"],["dc.bibliographiccitation.volume","1763"],["dc.contributor.author","Thoms, Sven"],["dc.contributor.author","Erdmann, Ralf"],["dc.date.accessioned","2020-08-10T05:25:21Z"],["dc.date.available","2020-08-10T05:25:21Z"],["dc.date.issued","2006"],["dc.description.abstract","The peroxisomal targeting signal type1 (PTS1) receptor Pex5 is required for the peroxisomal targeting of most matrix proteins. Pex5 recognises target proteins in the cytosol and directs them to the peroxisomal membrane where cargo is released into the matrix, and the receptor shuttles back to the cytosol. Recently, it has become evident that the membrane-bound Pex5 can be modified by mono- and polyubiquitination. This review summarises recent results on Pex5 ubiquitination and on the role of the AAA peroxins Pex1 and Pex6 as dislocases required for the release of Pex5 from the membrane to the cytosol where the receptor is either degraded by proteasomes or made available for another round of protein import into peroxisomes."],["dc.identifier.doi","10.1016/j.bbamcr.2006.08.046"],["dc.identifier.pmid","17028012"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/67543"],["dc.language.iso","en"],["dc.relation.issn","0006-3002"],["dc.title","Peroxisomal matrix protein receptor ubiquitination and recycling"],["dc.type","journal_article"],["dc.type.internalPublication","no"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","776"],["dc.bibliographiccitation.issue","6"],["dc.bibliographiccitation.journal","Eukaryotic Cell"],["dc.bibliographiccitation.lastpage","781"],["dc.bibliographiccitation.volume","10"],["dc.contributor.author","Debelyy, Mykhaylo O."],["dc.contributor.author","Thoms, Sven"],["dc.contributor.author","Connerth, Melanie"],["dc.contributor.author","Daum, Günther"],["dc.contributor.author","Erdmann, Ralf"],["dc.date.accessioned","2020-08-10T05:17:53Z"],["dc.date.available","2020-08-10T05:17:53Z"],["dc.date.issued","2011"],["dc.description.abstract","Here, we report the functional characterization of the newly identified lipid droplet hydrolase Ldh1p. Recombinant Ldh1p exhibits esterase and triacylglycerol lipase activities. Mutation of the serine in the hydrolase/lipase motif GXSXG completely abolished esterase activity. Ldh1p is required for the maintenance of a steady-state level of the nonpolar and polar lipids of lipid droplets. A characteristic feature of the Saccharomyces cerevisiae Δldh1 strain is the appearance of giant lipid droplets and an excessive accumulation of nonpolar lipids and phospholipids upon growth on medium containing oleic acid as a sole carbon source. Ldh1p is thought to play a role in maintaining the lipid homeostasis in yeast by regulating both phospholipid and nonpolar lipid levels."],["dc.identifier.doi","10.1128/EC.05040-11"],["dc.identifier.pmid","21478434"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/67539"],["dc.language.iso","en"],["dc.relation.eissn","1535-9786"],["dc.relation.issn","1535-9778"],["dc.title","Involvement of the Saccharomyces cerevisiae hydrolase Ldh1p in lipid homeostasis"],["dc.type","journal_article"],["dc.type.internalPublication","no"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","28223"],["dc.bibliographiccitation.issue","32"],["dc.bibliographiccitation.journal","The Journal of Biological Chemistry"],["dc.bibliographiccitation.lastpage","28234"],["dc.bibliographiccitation.volume","286"],["dc.contributor.author","Debelyy, Mykhaylo O."],["dc.contributor.author","Platta, Harald W."],["dc.contributor.author","Saffian, Delia"],["dc.contributor.author","Hensel, Astrid"],["dc.contributor.author","Thoms, Sven"],["dc.contributor.author","Meyer, Helmut E."],["dc.contributor.author","Warscheid, Bettina"],["dc.contributor.author","Girzalsky, Wolfgang"],["dc.contributor.author","Erdmann, Ralf"],["dc.date.accessioned","2020-08-10T05:15:59Z"],["dc.date.available","2020-08-10T05:15:59Z"],["dc.date.issued","2011"],["dc.description.abstract","Peroxisomal matrix protein import is facilitated by cycling receptors shuttling between the cytosol and the peroxisomal membrane. One crucial step in this cycle is the ATP-dependent release of the receptors from the peroxisomal membrane. This step is facilitated by the peroxisomal AAA (ATPases associated with various cellular activities) proteins Pex1p and Pex6p with ubiquitination of the receptor being the main signal for its export. Here we report that the AAA complex contains dislocase as well as deubiquitinating activity. Ubp15p, a ubiquitin hydrolase, was identified as a novel constituent of the complex. Ubp15p partially localizes to peroxisomes and is capable of cleaving off ubiquitin moieties from the type I peroxisomal targeting sequence (PTS1) receptor Pex5p. Furthermore, Ubp15p-deficient cells are characterized by a stress-related PTS1 import defect. The results merge into a picture in which removal of ubiquitin from the PTS1 receptor Pex5p is a specific event and might represent a vital step in receptor recycling."],["dc.identifier.doi","10.1074/jbc.M111.238600"],["dc.identifier.pmid","21665945"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/67538"],["dc.language.iso","en"],["dc.relation.eissn","1083-351X"],["dc.relation.issn","0021-9258"],["dc.title","Ubp15p, a ubiquitin hydrolase associated with the peroxisomal export machinery"],["dc.type","journal_article"],["dc.type.internalPublication","no"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","125"],["dc.bibliographiccitation.lastpage","134"],["dc.contributor.author","Thoms, Sven"],["dc.contributor.author","Erdmann, Ralf"],["dc.date.accessioned","2020-08-10T06:07:33Z"],["dc.date.available","2020-08-10T06:07:33Z"],["dc.date.issued","2005"],["dc.description.abstract","eroxisomes are organelles equipped with enzymes for lipid metabolism and hydrogen-peroxide-based respiration. Though many details of their metabolism are understood today, basic aspects concerning their biogenesis, including translocation of peroxisomal proteins into and through the peroxisomal membrane, still remain unknown. Nevertheless, the past years have brought forth a wealth of detailed information on the proteins required for proper biogenesis of peroxisomes. This review focuses on the basic principles and on recent developments in the field of peroxisome biogenesis. More comprehensive or specialized reviews can be found in the reference list."],["dc.identifier.doi","10.1007/0-387-30871-7_10"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/67556"],["dc.language.iso","en"],["dc.publisher","Springer"],["dc.publisher.place","Boston"],["dc.relation.eisbn","978-0-387-30871-5"],["dc.relation.isbn","978-0-387-25758-7"],["dc.relation.ispartof","rotein Movement Across Membranes. Molecular Biology Intelligence Unit"],["dc.title","Import of Proteins into Peroxisomes"],["dc.type","book_chapter"],["dc.type.internalPublication","no"],["dspace.entity.type","Publication"]]