title: Pichia pastoris Pex14p, a phosphorylated peroxisomal membrane protein, is part of a PTS-receptor docking complex and interacts with many peroxins.
abstract: The peroxisomal protein import machinery plays a central role in the assembly of this organelle in all eukaryotes. Genes encoding components of this machinery, termed peroxins or Pex proteins, have been isolated and characterized in several yeast species and in mammals, including humans. Here we report on one of these components, Pex14p, from the methylotrophic yeast Pichia pastoris. Work in other organisms has shown that Pex14p is located on the cytoplasmic surface of the peroxisomal membrane and binds peroxisomal targeting signal (PTS) receptors carrying proteins bound for the peroxisomal matrix, results that have led to the hypothesis that Pex14p is a receptor-docking protein. P. pastoris Pex14p (PpPex14p) behaves like an integral membrane protein, with its C-terminus exposed on the cytosolic side of the peroxisomal membrane. PpPex14p complexes with many peroxins, including Pex3p (Snyder et al., 1999b), Pex5p, Pex7p, Pex13p, Pex17p, itself, and a previously unreported peroxin, Pex8p. A portion of Pex14p is phosphorylated, but both phosphorylated and unphosphorylated forms of Pex14p interact with several peroxins. The interactions between Pex14p and other peroxins provide clues regarding the function of Pex14p in peroxisomal protein import.
authors.affiliation: Department of Biochemistry and Molecular Biology, Oregon Graduate Institute of Science and Technology, 20000 N.W. Walker Road, Beaverton, OR 97006-8921, USA.
authors.forename: M A
authors.initials: MA
authors.lastname: Johnson
authors.forename: W B
authors.initials: WB
authors.lastname: Snyder
authors.forename: J L
authors.initials: JL
authors.lastname: Cereghino
authors.forename: M
authors.initials: M
authors.lastname: Veenhuis
authors.forename: S
authors.initials: S
authors.lastname: Subramani
authors.forename: J M
authors.initials: JM
authors.lastname: Cregg
mesh_terms: D000595:Amino Acid Sequence; D000908:Antibodies, Fungal / Q000096:biosynthesis; D001483:Base Sequence; D002352:Carrier Proteins / Q000235:genetics* / Q000378:metabolism; D003001:Cloning, Molecular; D004271:DNA, Fungal / Q000737:chemistry / Q000302:isolation & purification; D008565:Membrane Proteins / Q000235:genetics* / Q000378:metabolism; D026901:Membrane Transport Proteins; D008854:Microscopy, Electron; D008969:Molecular Sequence Data; D016296:Mutagenesis; D000074401:Peroxins; D000074437:Peroxisomal Targeting Signal 2 Receptor; D000074435:Peroxisome-Targeting Signal 1 Receptor; D020675:Peroxisomes / Q000235:genetics* / Q000378:metabolism / Q000648:ultrastructure; D010766:Phosphorylation; D010843:Pichia / Q000235:genetics* / Q000378:metabolism / Q000648:ultrastructure; D010957:Plasmids; D016133:Polymerase Chain Reaction; D011233:Precipitin Tests; D018160:Receptors, Cytoplasmic and Nuclear / Q000378:metabolism*; D012097:Repressor Proteins; D029701:Saccharomyces cerevisiae Proteins; D016415:Sequence Alignment; D017422:Sequence Analysis, DNA; D017386:Sequence Homology, Amino Acid
chemical_list: D000908:Antibodies, Fungal; D002352:Carrier Proteins; D004271:DNA, Fungal; D008565:Membrane Proteins; D026901:Membrane Transport Proteins; C499195:PEX14 protein, S cerevisiae; D000074401:Peroxins; D000074437:Peroxisomal Targeting Signal 2 Receptor; D000074435:Peroxisome-Targeting Signal 1 Receptor; D018160:Receptors, Cytoplasmic and Nuclear; D012097:Repressor Proteins; D029701:Saccharomyces cerevisiae Proteins