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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 

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Degradation of the cleaved leader peptide of thiolase by a peroxisomal proteinase.

A peroxisomal location for insulin-degrading enzyme (IDE) has been defined by confocal immunofluorescence microscopy of stably transfected CHO cells overexpressing IDE and digitonin-permeabilization studies in normal nontransfected fibroblasts. The functional significance of IDE in degrading cleaved leader peptides of peroxisomal proteins targeted by the type II motif was evaluated with a synthetic peptide corresponding to the type II leader peptide of prethiolase. The peptide effectively competed for degradation and cross-linking of the high-affinity substrate 125I-labeled insulin to IDE. Direct proteolysis of the leader peptide of prethiolase was confirmed by HPLC; degradation was inhibited by immunodepletion with an antibody to IDE. Phylogenetic analysis of proteinases related to IDE revealed sequence similarity to mitochondrial processing peptidases.[1]

References

  1. Degradation of the cleaved leader peptide of thiolase by a peroxisomal proteinase. Authier, F., Bergeron, J.J., Ou, W.J., Rachubinski, R.A., Posner, B.I., Walton, P.A. Proc. Natl. Acad. Sci. U.S.A. (1995) [Pubmed]
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