Cookies on this website

We use cookies to ensure that we give you the best experience on our website. If you click 'Accept all cookies' we'll assume that you are happy to receive all cookies and you won't see this message again. If you click 'Reject all non-essential cookies' only necessary cookies providing core functionality such as security, network management, and accessibility will be enabled. Click 'Find out more' for information on how to change your cookie settings.

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




Journal article



Publication Date





2223 - 2229


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