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PEX13  -  Pex13p

Saccharomyces cerevisiae S288c

Synonyms: L9470.1, PAS20, Peroxin-13, Peroxisomal membrane protein PAS20, YLR191W
 
 
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High impact information on PEX13

  • Pex14p also interacts with two other membrane-bound peroxins including Pex13p, another binding protein for the PTS1 receptor [1].
  • Recently, many SH3 domains, including those from Grb2 and Pex13p, were reported to bind sequences lacking a PxxP motif [2].
  • The binding site of the Grb2 SH3 partially overlapped the conventional PxxP-binding site, whereas those of p67(phox) and Pex13p SH3s are located in different surface regions [2].
  • Pex13p is the putative docking protein for peroxisomal targeting signal 1 (PTS1)-dependent protein import into peroxisomes [3].
  • Reinvestigation of the topology revealed both termini of Pex13p to be oriented towards the cytosol [3].
 

Biological context of PEX13

 

Anatomical context of PEX13

  • 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 [8].
  • Subsequently, the formed Pex7p/cargo complex is transported from the cytosol to the peroxisomal docking complex, consisting of Pex13p and Pex14p [9].
  • A peroxisomally targeted Pex13p fragment became mislocalized to the endoplasmic reticulum in the absence of its Pex19p-binding site [10].
 

Physical interactions of PEX13

 

Other interactions of PEX13

  • Here we mapped the Pex7p interaction domain of Pex13p to its N-terminal 100 amino acids [9].
  • The pas (peroxisome assembly) mutants that have been used for complementation analysis represent 12 complementation groups including three novel ones, designated pas20, pas21 and pas22 [12].

References

  1. Pex14p, a peroxisomal membrane protein binding both receptors of the two PTS-dependent import pathways. Albertini, M., Rehling, P., Erdmann, R., Girzalsky, W., Kiel, J.A., Veenhuis, M., Kunau, W.H. Cell (1997) [Pubmed]
  2. Diverse recognition of non-PxxP peptide ligands by the SH3 domains from p67(phox), Grb2 and Pex13p. Kami, K., Takeya, R., Sumimoto, H., Kohda, D. EMBO J. (2002) [Pubmed]
  3. Involvement of Pex13p in Pex14p localization and peroxisomal targeting signal 2-dependent protein import into peroxisomes. Girzalsky, W., Rehling, P., Stein, K., Kipper, J., Blank, L., Kunau, W.H., Erdmann, R. J. Cell Biol. (1999) [Pubmed]
  4. The Arabidopsis pex12 and pex13 mutants are defective in both PTS1- and PTS2-dependent protein transport to peroxisomes. Mano, S., Nakamori, C., Nito, K., Kondo, M., Nishimura, M. Plant J. (2006) [Pubmed]
  5. 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, A.T., Kragt, A., Tabak, H.F., Distel, B. Mol. Biol. Cell (2000) [Pubmed]
  6. PEX13 is mutated in complementation group 13 of the peroxisome-biogenesis disorders. Liu, Y., Björkman, J., Urquhart, A., Wanders, R.J., Crane, D.I., Gould, S.J. Am. J. Hum. Genet. (1999) [Pubmed]
  7. The SH3 domain of the Saccharomyces cerevisiae peroxisomal membrane protein Pex13p functions as a docking site for Pex5p, a mobile receptor for the import PTS1-containing proteins. Elgersma, Y., Kwast, L., Klein, A., Voorn-Brouwer, T., van den Berg, M., Metzig, B., America, T., Tabak, H.F., Distel, B. J. Cell Biol. (1996) [Pubmed]
  8. Identification of Pex13p a peroxisomal membrane receptor for the PTS1 recognition factor. Erdmann, R., Blobel, G. J. Cell Biol. (1996) [Pubmed]
  9. Interactions of Pex7p and Pex18p/Pex21p with the peroxisomal docking machinery: implications for the first steps in PTS2 protein import. Stein, K., Schell-Steven, A., Erdmann, R., Rottensteiner, H. Mol. Cell. Biol. (2002) [Pubmed]
  10. Peroxisomal membrane proteins contain common Pex19p-binding sites that are an integral part of their targeting signals. Rottensteiner, H., Kramer, A., Lorenzen, S., Stein, K., Landgraf, C., Volkmer-Engert, R., Erdmann, R. Mol. Biol. Cell (2004) [Pubmed]
  11. Pex17p of Saccharomyces cerevisiae is a novel peroxin and component of the peroxisomal protein translocation machinery. Huhse, B., Rehling, P., Albertini, M., Blank, L., Meller, K., Kunau, W.H. J. Cell Biol. (1998) [Pubmed]
  12. An efficient positive selection procedure for the isolation of peroxisomal import and peroxisome assembly mutants of Saccharomyces cerevisiae. Elgersma, Y., van den Berg, M., Tabak, H.F., Distel, B. Genetics (1993) [Pubmed]
 
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