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    PEX14 peroxisomal biogenesis factor 14 [ Homo sapiens (human) ]

    Gene ID: 5195, updated on 12-Aug-2018

    GeneRIFs: Gene References Into Functions

    GeneRIFPubMed TitleDate
    Data suggest that soluble/cytosolic PEX5 interacts with PEX14/PEX13 complex, a model for the docking/translocation module (DTM) of the peroxisomal matrix protein translocon; PEX14/PEX13 complex appears to function in peroxisomal membrane as large cavity into which cytosolic PEX5 can enter to release its cargo. (PEX = peroxisomal biogenesis factor)

    The peroxisomal matrix protein translocon is a large cavity-forming protein assembly into which PEX5 protein enters to release its cargo.
    Dias AF, Rodrigues TA, Pedrosa AG, Barros-Barbosa A, Francisco T, Azevedo JE., Free PMC Article

    09/30/2017
    data reveal subpopulations of peroxisomes showing only weak colocalization between PEX14 and PEX5 or PEX11 but at the same time a clear compartmentalized organization. This compartmentalization, which was less evident in cases of strong colocalization, indicates dynamic protein reorganization linked to changes occurring in the peroxisomes.

    Super-resolution Microscopy Reveals Compartmentalization of Peroxisomal Membrane Proteins.
    Galiani S, Waithe D, Reglinski K, Cruz-Zaragoza LD, Garcia E, Clausen MP, Schliebs W, Erdmann R, Eggeling C., Free PMC Article

    05/6/2017
    PEX14 is the 13th PEX gene responsible for peroxisome biogenesis disorders. Thus far, only two patients with PEX14 deficiency have been reported.

    First Japanese case of Zellweger syndrome with a mutation in PEX14.
    Komatsuzaki S, Ogawa E, Shimozawa N, Sakamoto O, Haginoya K, Uematsu M, Hasegawa Y, Matsubara Y, Ohura T.

    01/28/2017
    The novel Pex14-binding site may represent the initial tethering site of Pex5 from which the cargo-loaded receptor is further processed in a sequential manner.

    A novel Pex14 protein-interacting site of human Pex5 is critical for matrix protein import into peroxisomes.
    Neuhaus A, Kooshapur H, Wolf J, Meyer NH, Madl T, Saidowsky J, Hambruch E, Lazam A, Jung M, Sattler M, Schliebs W, Erdmann R., Free PMC Article

    03/22/2014
    interaction of PEX5 with catalase and PEX14

    PEX5 protein binds monomeric catalase blocking its tetramerization and releases it upon binding the N-terminal domain of PEX14.
    Freitas MO, Francisco T, Rodrigues TA, Alencastre IS, Pinto MP, Grou CP, Carvalho AF, Fransen M, Sá-Miranda C, Azevedo JE., Free PMC Article

    01/21/2012
    PEX14 is a multi-tasking protein that not only facilitates peroxisomal protein import but is also required for peroxisome motility by serving as membrane anchor for microtubules.

    PEX14 is required for microtubule-based peroxisome motility in human cells.
    Bharti P, Schliebs W, Schievelbusch T, Neuhaus A, David C, Kock K, Herrmann C, Meyer HE, Wiese S, Warscheid B, Theiss C, Erdmann R.

    11/5/2011
    Observational study of gene-disease association, gene-environment interaction, and pharmacogenomic / toxicogenomic. (HuGE Navigator)

    Variation at the NFATC2 locus increases the risk of thiazolidinedione-induced edema in the Diabetes REduction Assessment with ramipril and rosiglitazone Medication (DREAM) study.
    Bailey SD, Xie C, Do R, Montpetit A, Diaz R, Mohan V, Keavney B, Yusuf S, Gerstein HC, Engert JC, Anand S, DREAM investigators.., Free PMC Article

    09/15/2010
    Observational study of gene-disease association. (HuGE Navigator)

    Gene-centric association signals for lipids and apolipoproteins identified via the HumanCVD BeadChip.
    Talmud PJ, Drenos F, Shah S, Shah T, Palmen J, Verzilli C, Gaunt TR, Pallas J, Lovering R, Li K, Casas JP, Sofat R, Kumari M, Rodriguez S, Johnson T, Newhouse SJ, Dominiczak A, Samani NJ, Caulfield M, Sever P, Stanton A, Shields DC, Padmanabhan S, Melander O, Hastie C, Delles C, Ebrahim S, Marmot MG, Smith GD, Lawlor DA, Munroe PB, Day IN, Kivimaki M, Whittaker J, Humphries SE, Hingorani AD, ASCOT investigators., NORDIL investigators., BRIGHT Consortium.., Free PMC Article

    09/15/2010
    Clinical trial of gene-disease association and gene-environment interaction. (HuGE Navigator)

    Personalized smoking cessation: interactions between nicotine dose, dependence and quit-success genotype score.
    Rose JE, Behm FM, Drgon T, Johnson C, Uhl GR., Free PMC Article

    06/30/2010
    analysis of the human Pex5.Pex14.PTS1 protein complex structure obtained by small angle X-ray scattering

    Solution structure of human Pex5.Pex14.PTS1 protein complexes obtained by small angle X-ray scattering.
    Shiozawa K, Konarev PV, Neufeld C, Wilmanns M, Svergun DI., Free PMC Article

    01/21/2010
    N-terminal domain of Pex14, Pex14(N), adopts a three-helical fold. Pex5 and Pex19 ligand helices bind competitively to the same surface in Pex14(N) albeit with opposite directionality.

    Structural basis for competitive interactions of Pex14 with the import receptors Pex5 and Pex19.
    Neufeld C, Filipp FV, Simon B, Neuhaus A, Schüller N, David C, Kooshapur H, Madl T, Erdmann R, Schliebs W, Wilmanns M, Sattler M., Free PMC Article

    01/21/2010
    This report represents the second PEX14-deficiency associated with Zellweger syndrome and the first documentation of a PEX14-deficient patient with detailed clinical follow-up and biochemical, morphological, and radiological data.

    Identification of a novel PEX14 mutation in Zellweger syndrome.
    Huybrechts SJ, Van Veldhoven PP, Hoffman I, Zeevaert R, de Vos R, Demaerel P, Brams M, Jaeken J, Fransen M, Cassiman D.

    01/21/2010
    a new complementation group of the peroxisome biogenesis disorders with PEX14 as the defective gene

    Identification of a new complementation group of the peroxisome biogenesis disorders and PEX14 as the mutated gene.
    Shimozawa N, Tsukamoto T, Nagase T, Takemoto Y, Koyama N, Suzuki Y, Komori M, Osumi T, Jeannette G, Wanders RJ, Kondo N.

    01/21/2010
    peroxisomal localization of Pex14p is affected by Pex13p

    Potential role for Pex19p in assembly of PTS-receptor docking complexes.
    Fransen M, Vastiau I, Brees C, Brys V, Mannaerts GP, Van Veldhoven PP.

    01/21/2010
    Serves as a transcriptional corepressor in addition to its peroxisomal function.

    NAPP2, a peroxisomal membrane protein, is also a transcriptional corepressor.
    Gavva NR, Wen SC, Daftari P, Moniwa M, Yang WM, Yang-Feng LP, Seto E, Davie JR, Shen CK.

    01/21/2010
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