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  1. Article: Peroxisomes: the extended shuttle to the peroxisome matrix.

    Kunau, W H

    Current biology : CB

    2001  Volume 11, Issue 16, Page(s) R659–62

    Abstract: A recent study indicates that protein import into the peroxisomal matrix occurs by a possibly unique mechanism involving the shuttling of cargo receptors into and out of the organelles. ...

    Abstract A recent study indicates that protein import into the peroxisomal matrix occurs by a possibly unique mechanism involving the shuttling of cargo receptors into and out of the organelles.
    MeSH term(s) Cell Line ; Genes, Reporter ; Humans ; Models, Biological ; Peroxisomal Targeting Signal 2 Receptor ; Peroxisome-Targeting Signal 1 Receptor ; Peroxisomes/metabolism ; Protein Transport/physiology ; Receptors, Cytoplasmic and Nuclear/metabolism ; Recombinant Fusion Proteins/metabolism ; Saccharomyces cerevisiae/physiology
    Chemical Substances Peroxisomal Targeting Signal 2 Receptor ; Peroxisome-Targeting Signal 1 Receptor ; Receptors, Cytoplasmic and Nuclear ; Recombinant Fusion Proteins
    Language English
    Publishing date 2001-08-21
    Publishing country England
    Document type Journal Article
    ZDB-ID 1071731-6
    ISSN 1879-0445 ; 0960-9822
    ISSN (online) 1879-0445
    ISSN 0960-9822
    DOI 10.1016/s0960-9822(01)00386-4
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    Zs.A 3208: Show issues Location:
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  2. Article: Peroxisome biogenesis: from yeast to man.

    Kunau, W H

    Current opinion in microbiology

    1998  Volume 1, Issue 2, Page(s) 232–237

    Abstract: A major current issue in studies of peroxisome biogenesis is how proteins are imported into the organelle or inserted into its membrane. Recent studies indicate that these two processes use independent pathways. Both appear to have unexpected properties. ...

    Abstract A major current issue in studies of peroxisome biogenesis is how proteins are imported into the organelle or inserted into its membrane. Recent studies indicate that these two processes use independent pathways. Both appear to have unexpected properties. Matrix proteins can be imported in an oligomeric form which might be facilitated by cycling receptors, whereas insertion of at least some peroxisomal membrane proteins seems to involve the endoplasmic reticulum.
    MeSH term(s) Biological Transport ; Endoplasmic Reticulum/metabolism ; Humans ; Intracellular Membranes/metabolism ; Membrane Proteins/metabolism ; Microbodies/metabolism ; Yeasts/genetics ; Yeasts/growth & development ; Yeasts/metabolism
    Chemical Substances Membrane Proteins
    Language English
    Publishing date 1998-04
    Publishing country England
    Document type Journal Article ; Research Support, Non-U.S. Gov't ; Review
    ZDB-ID 1418474-6
    ISSN 1879-0364 ; 1369-5274
    ISSN (online) 1879-0364
    ISSN 1369-5274
    DOI 10.1016/s1369-5274(98)80016-7
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  3. Article: PTS2 co-receptors: diverse proteins with common features.

    Schliebs, Wolfgang / Kunau, Wolf-H

    Biochimica et biophysica acta

    2006  Volume 1763, Issue 12, Page(s) 1605–1612

    Abstract: One feature of the PTS2 import pathway is the separation of the roles of the PTS receptor between two proteins. Pex7p alone is insufficient to act as the receptor for the import cycle for peroxisomal matrix proteins. In all cases, Pex7p needs a PTS2 co- ... ...

    Abstract One feature of the PTS2 import pathway is the separation of the roles of the PTS receptor between two proteins. Pex7p alone is insufficient to act as the receptor for the import cycle for peroxisomal matrix proteins. In all cases, Pex7p needs a PTS2 co-receptor to form an import-competent PTS2 receptor complex together with the PTS2 cargo. We provide an overview of the proteins that have been identified as PTS2 co-receptors and discuss their proposed functions.
    MeSH term(s) Amino Acid Sequence ; Animals ; Carrier Proteins/metabolism ; Carrier Proteins/physiology ; Consensus Sequence ; Fungal Proteins/physiology ; Humans ; Molecular Sequence Data ; Peroxisomal Targeting Signal 2 Receptor ; Peroxisomes/metabolism ; Protein Transport ; Receptors, Cytoplasmic and Nuclear/metabolism ; Receptors, Cytoplasmic and Nuclear/physiology
    Chemical Substances Carrier Proteins ; Fungal Proteins ; Peroxisomal Targeting Signal 2 Receptor ; Receptors, Cytoplasmic and Nuclear
    Language English
    Publishing date 2006-12
    Publishing country Netherlands
    Document type Journal Article ; Research Support, Non-U.S. Gov't ; Review
    ZDB-ID 60-7
    ISSN 1879-2596 ; 1879-260X ; 1872-8006 ; 1879-2642 ; 1879-2618 ; 1879-2650 ; 0006-3002 ; 0005-2728 ; 0005-2736 ; 0304-4165 ; 0167-4838 ; 1388-1981 ; 0167-4889 ; 0167-4781 ; 0304-419X ; 1570-9639 ; 0925-4439 ; 1874-9399
    ISSN (online) 1879-2596 ; 1879-260X ; 1872-8006 ; 1879-2642 ; 1879-2618 ; 1879-2650
    ISSN 0006-3002 ; 0005-2728 ; 0005-2736 ; 0304-4165 ; 0167-4838 ; 1388-1981 ; 0167-4889 ; 0167-4781 ; 0304-419X ; 1570-9639 ; 0925-4439 ; 1874-9399
    DOI 10.1016/j.bbamcr.2006.08.051
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  4. Article: Peroxisomal biogenesis in Saccharomyces cerevisiae.

    Kunau, W H

    Progress in clinical and biological research

    1992  Volume 375, Page(s) 9–18

    MeSH term(s) Fungal Proteins/genetics ; Genes, Fungal/genetics ; Microbodies/physiology ; Mutation/genetics ; Phenotype ; Saccharomyces cerevisiae/genetics ; Saccharomyces cerevisiae/ultrastructure
    Chemical Substances Fungal Proteins
    Language English
    Publishing date 1992
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't ; Review
    ISSN 0361-7742
    ISSN 0361-7742
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  5. Article: Peroxisome membrane biogenesis: the stage is set.

    Schliebs, Wolfgang / Kunau, Wolf-H

    Current biology : CB

    2004  Volume 14, Issue 10, Page(s) R397–9

    Abstract: Pex3p and Pex19p are key players in the post-translational import of peroxisomal membrane proteins. New data suggest that these peroxins act in tandem, Pex19p as a cytosolic chaperone and import receptor for peroxisomal membrane proteins, and Pex3p as ... ...

    Abstract Pex3p and Pex19p are key players in the post-translational import of peroxisomal membrane proteins. New data suggest that these peroxins act in tandem, Pex19p as a cytosolic chaperone and import receptor for peroxisomal membrane proteins, and Pex3p as docking factor at the peroxisomal membrane.
    MeSH term(s) Biological Transport ; Intracellular Membranes/metabolism ; Membrane Proteins/genetics ; Membrane Proteins/metabolism ; Models, Biological ; Molecular Chaperones/genetics ; Molecular Chaperones/metabolism ; Peroxins ; Peroxisomes/genetics ; Peroxisomes/metabolism ; Saccharomyces cerevisiae Proteins/genetics ; Saccharomyces cerevisiae Proteins/metabolism
    Chemical Substances Membrane Proteins ; Molecular Chaperones ; PEX3 protein, S cerevisiae ; Peroxins ; Saccharomyces cerevisiae Proteins
    Language English
    Publishing date 2004-05-25
    Publishing country England
    Document type Journal Article ; Review
    ZDB-ID 1071731-6
    ISSN 1879-0445 ; 0960-9822
    ISSN (online) 1879-0445
    ISSN 0960-9822
    DOI 10.1016/j.cub.2004.05.017
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  6. Article: The diversity of organelle protein import mechanisms.

    Kunau, W H / Agne, B / Girzalsky, W

    Trends in cell biology

    2003  Volume 11, Issue 9, Page(s) 358–361

    Abstract: It was once believed that common mechanisms underpin the transfer of proteins across the membrane systems of organelles such as mitochondria, chloroplasts and peroxisomes. Now that many of the core components of the translocases have been indentified, ... ...

    Abstract It was once believed that common mechanisms underpin the transfer of proteins across the membrane systems of organelles such as mitochondria, chloroplasts and peroxisomes. Now that many of the core components of the translocases have been indentified, results discussed at a recent conference [Max-Delbrück-Centrum Symposium "Protein Transport and Stability"; Berlin, Germany; 21-26 March 2001. Organized by Thomas Sommer and Enno Hartmann.] stress just how diverse the mechanisms of transport into these organelles really are.
    MeSH term(s) Carrier Proteins/metabolism ; Chloroplasts/metabolism ; Endocytosis/physiology ; Membrane Proteins/metabolism ; Mitochondria/metabolism ; Models, Biological ; Peroxisomes/metabolism ; Protein Transport/physiology
    Chemical Substances Carrier Proteins ; Membrane Proteins
    Language English
    Publishing date 2003-02-19
    Publishing country England
    Document type Journal Article
    ZDB-ID 30122-x
    ISSN 1879-3088 ; 0962-8924
    ISSN (online) 1879-3088
    ISSN 0962-8924
    DOI 10.1016/s0962-8924(01)02083-9
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    Zs.MG 25: Show issues
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    Zs.A 3410: Show issues Location:
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  7. Article: Peroxisome biogenesis: back to the endoplasmic reticulum?

    Kunau, W H / Erdmann, R

    Current biology : CB

    1998  Volume 8, Issue 9, Page(s) R299–302

    Abstract: Proteins are targeted to the membrane and matrix of peroxisomes by distinct pathways. Recent observations suggest a further route: a subset of peroxisomal membrane proteins might be targeted first to the endoplasmic reticulum, and from there to ... ...

    Abstract Proteins are targeted to the membrane and matrix of peroxisomes by distinct pathways. Recent observations suggest a further route: a subset of peroxisomal membrane proteins might be targeted first to the endoplasmic reticulum, and from there to peroxisomes by vesicle-mediated transport.
    MeSH term(s) Animals ; Biological Transport, Active ; Coatomer Protein ; Endoplasmic Reticulum/metabolism ; Glycosylation ; Humans ; Liver/metabolism ; Membrane Proteins/metabolism ; Microbodies/metabolism ; Models, Biological ; Phosphoproteins/metabolism ; Protein Binding ; Saccharomyces cerevisiae Proteins
    Chemical Substances Coatomer Protein ; Membrane Proteins ; PEX15 protein, S cerevisiae ; Phosphoproteins ; Saccharomyces cerevisiae Proteins
    Language English
    Publishing date 1998-04-23
    Publishing country England
    Document type Journal Article ; Research Support, Non-U.S. Gov't ; Review
    ZDB-ID 1071731-6
    ISSN 1879-0445 ; 0960-9822
    ISSN (online) 1879-0445
    ISSN 0960-9822
    DOI 10.1016/s0960-9822(98)70191-5
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  8. Article: Protein import into peroxisomes: an exception to the rule?

    Huhse, B / Kunau, W H

    Cold Spring Harbor symposia on quantitative biology

    1995  Volume 60, Page(s) 657–662

    MeSH term(s) Biological Transport, Active ; Humans ; Microbodies/metabolism ; Models, Biological ; Peroxisomal Disorders/metabolism ; Peroxisomal Targeting Signal 2 Receptor ; Peroxisome-Targeting Signal 1 Receptor ; Proteins/metabolism ; Receptors, Cytoplasmic and Nuclear/metabolism
    Chemical Substances Peroxisomal Targeting Signal 2 Receptor ; Peroxisome-Targeting Signal 1 Receptor ; Proteins ; Receptors, Cytoplasmic and Nuclear
    Language English
    Publishing date 1995
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't ; Review
    ISSN 0091-7451
    ISSN 0091-7451
    DOI 10.1101/sqb.1995.060.01.070
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  9. Article: Purification and immunolocalization of the peroxisomal 3-oxoacyl-CoA thiolase from Saccharomyces cerevisiae.

    Erdmann, R / Kunau, W H

    Yeast (Chichester, England)

    1994  Volume 10, Issue 9, Page(s) 1173–1182

    Abstract: A molecular understanding of peroxisome biogenesis depends upon the analysis of peroxisomal proteins. Here we describe the isolation of the 3-oxoacyl-CoA thiolase of the peroxisomal beta-oxidation system from Saccharomyces cerevisiae as a dimer of ... ...

    Abstract A molecular understanding of peroxisome biogenesis depends upon the analysis of peroxisomal proteins. Here we describe the isolation of the 3-oxoacyl-CoA thiolase of the peroxisomal beta-oxidation system from Saccharomyces cerevisiae as a dimer of identical subunits, each with a molecular mass of 45 kDa. Monospecific polyclonal antibodies were raised against the purified enzyme, and its peroxisomal origin was demonstrated by immunoblotting of subcellular fractions as well as by immunogold labelling. We also show that these antibodies could be suitable for an immunofluorescence microscopy screening of yeast mutants affected in peroxisome assembly.
    MeSH term(s) Acetyl-CoA C-Acyltransferase/analysis ; Acetyl-CoA C-Acyltransferase/immunology ; Acetyl-CoA C-Acyltransferase/isolation & purification ; Animals ; Antibodies/analysis ; Male ; Microbodies/enzymology ; Microbodies/genetics ; Microscopy, Fluorescence ; Microscopy, Immunoelectron ; Rabbits ; Saccharomyces cerevisiae/enzymology ; Saccharomyces cerevisiae/genetics ; Saccharomyces cerevisiae/ultrastructure
    Chemical Substances Antibodies ; Acetyl-CoA C-Acyltransferase (EC 2.3.1.16)
    Language English
    Publishing date 1994-09
    Publishing country England
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 632636-5
    ISSN 1097-0061 ; 0749-503X
    ISSN (online) 1097-0061
    ISSN 0749-503X
    DOI 10.1002/yea.320100905
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  10. Article ; Online: Pex17p-dependent assembly of Pex14p/Dyn2p-subcomplexes of the peroxisomal protein import machinery.

    Chan, Anna / Schummer, Andreas / Fischer, Sven / Schröter, Thomas / Cruz-Zaragoza, Luis Daniel / Bender, Julian / Drepper, Friedel / Oeljeklaus, Silke / Kunau, Wolf-H / Girzalsky, Wolfgang / Warscheid, Bettina / Erdmann, Ralf

    European journal of cell biology

    2016  Volume 95, Issue 12, Page(s) 585–597

    Abstract: Peroxisomal matrix protein import is facilitated by cycling receptors that recognize their cargo proteins in the cytosol by peroxisomal targeting sequences (PTS). In the following, the assembled receptor-cargo complex is targeted to the peroxisomal ... ...

    Abstract Peroxisomal matrix protein import is facilitated by cycling receptors that recognize their cargo proteins in the cytosol by peroxisomal targeting sequences (PTS). In the following, the assembled receptor-cargo complex is targeted to the peroxisomal membrane where it docks to the docking-complex as part of the peroxisomal translocation machinery. The docking-complex is composed of Pex13p, Pex14p and in yeast also Pex17p, whose function is still elusive. In order to characterize the function of Pex17p, we compared the composition and size of peroxisomal receptor-docking complexes from wild-type and pex17Δ cells. Our data demonstrate that the deficiency of Pex17p affects the stoichiometry of the constituents of an isolated 600kDa complex and that pex17Δ cells lack a high molecular weight complex (>900kDa) of unknown function. We identified the dynein light chain protein Dyn2p as an additional core component of the Pex14p/Pex17p-complex. Both, Pex14p and Pex17p interact directly with Dyn2p, but in vivo, Pex17p turned out to be prerequisite for an association of Dyn2p with Pex14p. Finally, like pex17Δ also dyn2Δ cells lack the high molecular weight complex. As dyn2Δ cells also display reduced peroxisomal function, our data indicate that Dyn2p-dependent formation of the high molecular weight Pex14p-complex is required to maintain peroxisomal function on wild-type level.
    MeSH term(s) Dyneins/genetics ; Dyneins/metabolism ; Membrane Transport Proteins/genetics ; Membrane Transport Proteins/metabolism ; Multiprotein Complexes/genetics ; Multiprotein Complexes/metabolism ; Peroxins ; Peroxisomes/genetics ; Peroxisomes/metabolism ; Protein Transport/physiology ; Repressor Proteins/genetics ; Repressor Proteins/metabolism ; Saccharomyces cerevisiae/genetics ; Saccharomyces cerevisiae/metabolism ; Saccharomyces cerevisiae Proteins/genetics ; Saccharomyces cerevisiae Proteins/metabolism
    Chemical Substances Membrane Transport Proteins ; Multiprotein Complexes ; PEX14 protein, S cerevisiae ; PEX17 protein, S cerevisiae ; Peroxins ; Repressor Proteins ; Saccharomyces cerevisiae Proteins ; Dyneins (EC 3.6.4.2) ; SLC1 protein, S cerevisiae (EC 3.6.4.2)
    Language English
    Publishing date 2016-12
    Publishing country Germany
    Document type Journal Article
    ZDB-ID 391967-5
    ISSN 1618-1298 ; 0070-2463 ; 0171-9335
    ISSN (online) 1618-1298
    ISSN 0070-2463 ; 0171-9335
    DOI 10.1016/j.ejcb.2016.10.004
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