|Title||Protein translocation into peroxisomes by ring-shaped import receptors|
|Publication Type||Journal Article|
|Year of Publication||2007|
|Authors||Stanley, WA, Fodor, K, Marti-Renom, MA, Schliebs, W, Wilmanns, M|
|Keywords||Amino Acid Sequence Binding Sites Humans Molecular Sequence Data Peroxisomes/*metabolism Protein Structure; Cytoplasmic and Nuclear/*chemistry; Tertiary Protein Transport Receptors|
Folded and functional proteins destined for translocation from the cytosol into the peroxisomal matrix are recognized by two different peroxisomal import receptors, Pex5p and Pex7p. Both cargo-loaded receptors dock on the same translocon components, followed by cargo release and receptor recycling, as part of the complete translocation process. Recent structural and functional evidence on the Pex5p receptor has provided insight on the molecular requirements of specific cargo recognition, while the remaining processes still remain largely elusive. Comparison of experimental structures of Pex5p and a structural model of Pex7p reveal that both receptors are built by ring-like arrangements with cargo binding sites, central to the respective structures. Although, molecular insight into the complete peroxisomal translocon still remains to be determined, emerging data allow to deduce common molecular principles that may hold for other translocation systems as well.
Stanley, Will A Fodor, Krisztian Marti-Renom, Marc A Schliebs, Wolfgang Wilmanns, Matthias Review Netherlands FEBS letters FEBS Lett. 2007 Oct 16;581(25):4795-802. Epub 2007 Sep 11.