Thoms, Sven

[["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","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"]]