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PEX5 acts as a cycling receptor for import of PTS1 proteins into peroxisomes and as a co-receptor for PEX7, the PTS2 receptor, but the mechanism of cargo unloading has remained obscure. Using recombinant protein domains we show PEX5 binding to the PEX14N-terminal domain (PEX14N) has no effect on the affinity of PEX5 for a PTS1 containing peptide. PEX5 can form a complex containing both recombinant PTS1 cargo and endogenous PEX7-thiolase simultaneously but isolation of the complex via the PEX14 construct resulted in an absence of thiolase, suggesting a possible role for PEX14 in the unloading of PTS2 cargos.

Original publication

DOI

10.1016/j.febslet.2014.05.038

Type

Journal article

Journal

FEBS Lett

Publication Date

2014

Volume

588

Pages

2223 - 2229

Keywords

Arabidopsis/*metabolism Arabidopsis Proteins/*metabolism Kinetics Membrane Proteins/*metabolism Peroxisomal Targeting Signal 2 Receptor Peroxisome-Targeting Signal 1 Receptor Protein Binding Protein Transport Receptors, Cytoplasmic and Nuclear/*metabolism Repressor Proteins/*metabolism Arabidopsis thaliana Cargo unloading Pex14 Pex5 Pex7 Pts1 Pts2 Peroxisome