%0 Journal Article %1 grouMembersE2DUbcH52008 %A Grou, Cláudia P. %A Carvalho, Andreia F. %A Pinto, Manuel P. %A Wiese, Sebastian %A Piechura, Heike %A Meyer, Helmut E. %A Warscheid, Bettina %A Sá-Miranda, Clara %A Azevedo, Jorge E. %C United States %D 2008 %J The Journal of biological chemistry %K 1 Animals,Cells Cultured,Cysteine/genetics/metabolism,Cytosol/metabolism,Gene Cytoplasmic Deletion,Humans,Male,Membrane Enzymes/classification/genetics/*metabolism,Ubiquitination Isoforms/genetics/metabolism,Protein Nuclear/genetics/*metabolism,Recombinant Proteins/genetics/*metabolism,Peroxisome-Targeting Proteins/genetics/metabolism,Saccharomyces Receptor,Peroxisomes/*metabolism,Protein Signal Transport Transport,Rats,Receptors and cerevisiae cerevisiae/genetics/metabolism,to_read,Ubiquitin-Conjugating %N 21 %P 14190--14197 %R 10.1074/jbc.M800402200 %T Members of the E2D (UbcH5) Family Mediate the Ubiquitination of the Conserved Cysteine of Pex5p, the Peroxisomal Import Receptor. %V 283 %X According to current models of peroxisomal biogenesis, newly synthesized peroxisomal matrix proteins are transported into the organelle by Pex5p. Pex5p recognizes these proteins in the cytosol, mediates their membrane translocation, and is exported back into the cytosol in an ATP-dependent manner. We have previously shown that export of Pex5p is preceded by (and requires) monoubiquitination of a conserved cysteine residue present at its N terminus. In yeasts, and probably also in plants, ubiquitination of Pex5p is mediated by a specialized ubiquitin-conjugating enzyme, Pex4p. In mammals, the identity of this enzyme has remained unknown for many years. Here, we provide evidence suggesting that E2D1/2/3 (UbcH5a/b/c) are the mammalian functional counterparts of yeast/plant Pex4p. The mechanistic implications of these findings are discussed.

@article{grouMembersE2DUbcH52008, abstract = {According to current models of peroxisomal biogenesis, newly synthesized peroxisomal matrix proteins are transported into the organelle by Pex5p. Pex5p recognizes these proteins in the cytosol, mediates their membrane translocation, and is exported back into the cytosol in an ATP-dependent manner. We have previously shown that export of Pex5p is preceded by (and requires) monoubiquitination of a conserved cysteine residue present at its N terminus. In yeasts, and probably also in plants, ubiquitination of Pex5p is mediated by a specialized ubiquitin-conjugating enzyme, Pex4p. In mammals, the identity of this enzyme has remained unknown for many years. Here, we provide evidence suggesting that E2D1/2/3 (UbcH5a/b/c) are the mammalian functional counterparts of yeast/plant Pex4p. The mechanistic implications of these findings are discussed.}, added-at = {2024-05-17T13:01:35.000+0200}, address = {United States}, author = {Grou, Cl{\'a}udia P. and Carvalho, Andreia F. and Pinto, Manuel P. and Wiese, Sebastian and Piechura, Heike and Meyer, Helmut E. and Warscheid, Bettina and {S{\'a}-Miranda}, Clara and Azevedo, Jorge E.}, biburl = {https://www.bibsonomy.org/bibtex/2324d0fa779b7dbfa9ef1a9cee1ccb86d/warscheidlab}, doi = {10.1074/jbc.M800402200}, interhash = {1322903800ea81cccd890e1358f06698}, intrahash = {324d0fa779b7dbfa9ef1a9cee1ccb86d}, issn = {0021-9258}, journal = {The Journal of biological chemistry}, keywords = {1 Animals,Cells Cultured,Cysteine/genetics/metabolism,Cytosol/metabolism,Gene Cytoplasmic Deletion,Humans,Male,Membrane Enzymes/classification/genetics/*metabolism,Ubiquitination Isoforms/genetics/metabolism,Protein Nuclear/genetics/*metabolism,Recombinant Proteins/genetics/*metabolism,Peroxisome-Targeting Proteins/genetics/metabolism,Saccharomyces Receptor,Peroxisomes/*metabolism,Protein Signal Transport Transport,Rats,Receptors and cerevisiae cerevisiae/genetics/metabolism,to_read,Ubiquitin-Conjugating}, langid = {english}, month = may, number = 21, pages = {14190--14197}, pmid = {18359941}, timestamp = {2024-05-17T13:01:35.000+0200}, title = {Members of the {{E2D}} ({{UbcH5}}) Family Mediate the Ubiquitination of the Conserved Cysteine of {{Pex5p}}, the Peroxisomal Import Receptor.}, volume = 283, year = 2008 }