PTS1-independent sorting of peroxisomal matrix proteins by Pex5p.

Marten Veenhuis, Ida J van der Klei

Journal: Biochimica et biophysica acta 2007;1763(12):1794-800

PMID: 17005270

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Abstract

Most peroxisomal matrix proteins contain a peroxisomal targeting signal 1 (PTS1) for sorting to the correct organelle. This signal is located at the extreme C-terminus and generally consists of only three amino acids. The PTS1 is recognized by the receptor protein Pex5p. Several examples have been reported of peroxisomal matrix proteins that are sorted to peroxisomes via Pex5p, but lack a typical PTS1 tripeptide. In this contribution we present an overview of these so-called non-PTS1 proteins and discuss the current knowledge of the molecular mechanisms involved in their sorting.

Address: Eukaryotic Microbiology, Groningen Biomolecular Sciences and Biotechnology Institute (GBB), University of Groningen, The Netherlands. [email protected]

DOI: 10.1016/j.bbamcr.2006.08.013

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MeSH Terms: Acyl-CoA Oxidase, Alanine Transaminase, Alcohol Oxidoreductases, Carnitine O-Acetyltransferase, Fungal Proteins, Humans, Peroxisome-Targeting Signal 1 Receptor, Peroxisomes, Protein Sorting Signals, Protein Transport, Receptors, Cytoplasmic and Nuclear