We identified a Saccharomyces cerevisiae peroxisomal membrane protein, Pex13p, that is essential for protein import. A point mutation in the COOH-terminal Src homology 3 (SH3) domain of Pex13p inactivated the protein but did not affect its membrane targeting. A two-hybrid screen with the SH3 domain of Pex13p identified Pex5p, a receptor for proteins with a type I peroxisomal targeting signal (PTS1), as its ligand. Pex13p SH3 interacted specifically with Pex5p in vitro. We determined, furthermore, that Pex5p was mainly present in the cytosol and only a small fraction was associated with peroxisomes. We therefore propose that Pex13p is a component of the peroxisomal protein import machinery onto which the mobile Pex5p receptor docks for the delivery of the selected PTS1 protein.
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1 October 1996
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October 01 1996
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.
Y Elgersma,
Y Elgersma
Department of Biochemistry, Academic Medical Centre, Amsterdam, The Netherlands.
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L Kwast,
L Kwast
Department of Biochemistry, Academic Medical Centre, Amsterdam, The Netherlands.
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A Klein,
A Klein
Department of Biochemistry, Academic Medical Centre, Amsterdam, The Netherlands.
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T Voorn-Brouwer,
T Voorn-Brouwer
Department of Biochemistry, Academic Medical Centre, Amsterdam, The Netherlands.
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M van den Berg,
M van den Berg
Department of Biochemistry, Academic Medical Centre, Amsterdam, The Netherlands.
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B Metzig,
B Metzig
Department of Biochemistry, Academic Medical Centre, Amsterdam, The Netherlands.
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T America,
T America
Department of Biochemistry, Academic Medical Centre, Amsterdam, The Netherlands.
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H F Tabak,
H F Tabak
Department of Biochemistry, Academic Medical Centre, Amsterdam, The Netherlands.
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B Distel
B Distel
Department of Biochemistry, Academic Medical Centre, Amsterdam, The Netherlands.
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Y Elgersma
Department of Biochemistry, Academic Medical Centre, Amsterdam, The Netherlands.
L Kwast
Department of Biochemistry, Academic Medical Centre, Amsterdam, The Netherlands.
A Klein
Department of Biochemistry, Academic Medical Centre, Amsterdam, The Netherlands.
T Voorn-Brouwer
Department of Biochemistry, Academic Medical Centre, Amsterdam, The Netherlands.
M van den Berg
Department of Biochemistry, Academic Medical Centre, Amsterdam, The Netherlands.
B Metzig
Department of Biochemistry, Academic Medical Centre, Amsterdam, The Netherlands.
T America
Department of Biochemistry, Academic Medical Centre, Amsterdam, The Netherlands.
H F Tabak
Department of Biochemistry, Academic Medical Centre, Amsterdam, The Netherlands.
B Distel
Department of Biochemistry, Academic Medical Centre, Amsterdam, The Netherlands.
Online ISSN: 1540-8140
Print ISSN: 0021-9525
J Cell Biol (1996) 135 (1): 97–109.
Citation
Y Elgersma, L Kwast, A Klein, T Voorn-Brouwer, M van den Berg, B Metzig, T America, H F Tabak, B Distel; 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.. J Cell Biol 1 October 1996; 135 (1): 97–109. doi: https://doi.org/10.1083/jcb.135.1.97
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