Import of newly synthesized PTS1 proteins into the peroxisome requires the PTS1 receptor (Pex5p), a predominantly cytoplasmic protein that cycles between the cytoplasm and peroxisome. We have identified Pex13p, a novel integral peroxisomal membrane from both yeast and humans that binds the PTS1 receptor via a cytoplasmically oriented SH3 domain. Although only a small amount of Pex5p is bound to peroxisomes at steady state (< 5%), loss of Pex13p further reduces the amount of peroxisome-associated Pex5p by approximately 40-fold. Furthermore, loss of Pex13p eliminates import of peroxisomal matrix proteins that contain either the type-1 or type-2 peroxisomal targeting signal but does not affect targeting and insertion of integral peroxisomal membrane proteins. We conclude that Pex13p functions as a docking factor for the predominantly cytoplasmic PTS1 receptor.
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1 October 1996
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October 01 1996
Pex13p is an SH3 protein of the peroxisome membrane and a docking factor for the predominantly cytoplasmic PTs1 receptor.
S J Gould,
S J Gould
Department of Biological Chemistry, Johns Hopkins University School of Medicine, Kennedy Krieger Institute, Baltimore, Maryland 21205, USA. [email protected]
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J E Kalish,
J E Kalish
Department of Biological Chemistry, Johns Hopkins University School of Medicine, Kennedy Krieger Institute, Baltimore, Maryland 21205, USA. [email protected]
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J C Morrell,
J C Morrell
Department of Biological Chemistry, Johns Hopkins University School of Medicine, Kennedy Krieger Institute, Baltimore, Maryland 21205, USA. [email protected]
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J Bjorkman,
J Bjorkman
Department of Biological Chemistry, Johns Hopkins University School of Medicine, Kennedy Krieger Institute, Baltimore, Maryland 21205, USA. [email protected]
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A J Urquhart,
A J Urquhart
Department of Biological Chemistry, Johns Hopkins University School of Medicine, Kennedy Krieger Institute, Baltimore, Maryland 21205, USA. [email protected]
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D I Crane
D I Crane
Department of Biological Chemistry, Johns Hopkins University School of Medicine, Kennedy Krieger Institute, Baltimore, Maryland 21205, USA. [email protected]
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S J Gould
Department of Biological Chemistry, Johns Hopkins University School of Medicine, Kennedy Krieger Institute, Baltimore, Maryland 21205, USA. [email protected]
J E Kalish
Department of Biological Chemistry, Johns Hopkins University School of Medicine, Kennedy Krieger Institute, Baltimore, Maryland 21205, USA. [email protected]
J C Morrell
Department of Biological Chemistry, Johns Hopkins University School of Medicine, Kennedy Krieger Institute, Baltimore, Maryland 21205, USA. [email protected]
J Bjorkman
Department of Biological Chemistry, Johns Hopkins University School of Medicine, Kennedy Krieger Institute, Baltimore, Maryland 21205, USA. [email protected]
A J Urquhart
Department of Biological Chemistry, Johns Hopkins University School of Medicine, Kennedy Krieger Institute, Baltimore, Maryland 21205, USA. [email protected]
D I Crane
Department of Biological Chemistry, Johns Hopkins University School of Medicine, Kennedy Krieger Institute, Baltimore, Maryland 21205, USA. [email protected]
Online ISSN: 1540-8140
Print ISSN: 0021-9525
J Cell Biol (1996) 135 (1): 85–95.
Citation
S J Gould, J E Kalish, J C Morrell, J Bjorkman, A J Urquhart, D I Crane; Pex13p is an SH3 protein of the peroxisome membrane and a docking factor for the predominantly cytoplasmic PTs1 receptor.. J Cell Biol 1 October 1996; 135 (1): 85–95. doi: https://doi.org/10.1083/jcb.135.1.85
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