Identification of Pex13p, a peroxisomal membrane receptor for the PTS1 recognition factor

被引:179
|
作者
Erdmann, R [1 ]
Blobel, G [1 ]
机构
[1] ROCKEFELLER UNIV, HOWARD HUGHES MED INST, CELL BIOL LAB, NEW YORK, NY 10021 USA
来源
JOURNAL OF CELL BIOLOGY | 1996年 / 135卷 / 01期
关键词
D O I
10.1083/jcb.135.1.111
中图分类号
Q2 [细胞生物学];
学科分类号
071009 ; 090102 ;
摘要
We have identified an S. cerevisiae integral peroxisomal membrane protein of M(r) of 42,705 (Pex13p) that is a component of the peroxisomal protein import apparatus. Pex13p's most striking feature is an src homology 3 (SH3) domain that interacts directly with yeast Pex5p (former Pas10p), the recognition factor for the COOH-terminal tripeptide signal sequence (PTS1), but not with Pex7p (former Pas7p), the recognition factor for the NH2-terminal nonapeptide signal (PTS2) of peroxisomal matrix proteins. Hence, Pex13p serves as peroxisomal membrane receptor for at least one of the two peroxisomal signal recognition factors. Cells deficient in Pex13p are unable to import peroxisomal matrix proteins containing PTS1 and, surprisingly, also those containing PTS2. Pex13p deficient cells retain membranes containing the peroxisomal membrane protein Pex11p (former Pmp27p), consistent with the existence of independent pathways for the integration of peroxisomal membrane proteins and for the translocation of peroxisomal matrix proteins.
引用
收藏
页码:111 / 121
页数:11
相关论文
共 50 条
  • [1] Pex13p is an SH3 protein of the peroxisome membrane and a docking factor for the predominantly cytoplasmic PTS1 receptor
    Gould, SJ
    Kalish, JE
    Morrell, JC
    Bjorkman, J
    Urquhart, AJ
    Crane, DI
    JOURNAL OF CELL BIOLOGY, 1996, 135 (01): : 85 - 95
  • [2] Saccharomyces cerevisiae PTS1 receptor Pex5p interacts with the SH3 domain of the peroxisomal membrane protein Pex13p in an unconventional, non-PXXP-related manner
    Bottger, G
    Barnett, P
    Klein, ATJ
    Kragt, A
    Tabak, HF
    Distel, B
    MOLECULAR BIOLOGY OF THE CELL, 2000, 11 (11) : 3963 - 3976
  • [3] Interaction of Pex5p, the type 1 peroxisome targeting signal receptor, with the peroxisomal membrane proteins Pex14p and Pex13p
    Urquhart, AJ
    Kennedy, D
    Gould, SJ
    Crane, DI
    JOURNAL OF BIOLOGICAL CHEMISTRY, 2000, 275 (06) : 4127 - 4136
  • [4] A novel, non-PTS1, peroxisomal import route dependent on the PTS1 receptor Pex5p.
    Skoneczny, M
    Lazarow, PB
    MOLECULAR BIOLOGY OF THE CELL, 1998, 9 : 348A - 348A
  • [5] Peroxisomal PTS1 and PTS2 protein import is mediated by distinct domains of the human PTS1 receptor PEX5.
    Dodt, G
    Warren, D
    Yahraus, T
    Soukupova, M
    Becker, E
    Moellers, B
    Rehling, P
    Gould, SJ
    MOLECULAR BIOLOGY OF THE CELL, 1998, 9 : 349A - 349A
  • [6] The SH3 domain of the Saccharomyces cerevisiae peroxisomal membrane protein Pex13p functions as a docking site for Pex5p, a mobile receptor for the import of PTS1-containing proteins
    Elgersma, Y
    Kwast, L
    Klein, A
    VoornBrouwer, T
    vandenBerg, M
    Metzig, B
    America, T
    Tabak, HF
    Distel, B
    JOURNAL OF CELL BIOLOGY, 1996, 135 (01): : 97 - 109
  • [7] The peroxisomal membrane protein Pex13p shows a novel mode of SH3 interaction
    Barnett, P
    Bottger, G
    Klein, ATJ
    Tabak, HF
    Distel, B
    EMBO JOURNAL, 2000, 19 (23): : 6382 - 6391
  • [8] Functional similarity between the peroxisomal PTS2 receptor binding protein Pex18p and the N-terminal half of the PTS1 receptor Pex5p
    Schäfer, A
    Kerssen, D
    Veenhuis, M
    Kunau, WH
    Schliebs, W
    MOLECULAR AND CELLULAR BIOLOGY, 2004, 24 (20) : 8895 - 8906
  • [9] Peroxisomal matrix protein importSuppression of protein import defects in Hansenula polymorpha pex Mutants by Overproduction of the PTS1 Receptor Pex5p
    Jan A. K. W. Kiel
    Marten Veenhuis
    Cell Biochemistry and Biophysics, 2000, 32 : 9 - 19
  • [10] Functional characterization of Pex13p, an essential component of the peroxisomal docking complex
    Stein, K
    Hong, XJ
    Schneider-Mergener, J
    Erdmann, R
    MOLECULAR BIOLOGY OF THE CELL, 2000, 11 : 423A - 424A