Plant Physiology Preview
Published on September 16, 2005; 10.1104/pp.105.065094
Received May 10, 2005
Returned for revision July 4, 2005
Accepted July 18, 2005
AtPEX2 and AtPEX10 Are Targeted to Peroxisomes Independently of Known Endoplasmic Reticulum Trafficking Routes
Imogen Averil Sparkes *, Chris Hawes , and Alison Baker
School of Biological and Molecular Sciences, Oxford Brookes University, Oxford 0X3 0BP, United Kingdom
Centre for Plant Sciences, University of Leeds, Leeds LS2 9JT, United Kingdom
* Corresponding author; email: isparkes{at}brookes.ac.uk.
Controversy exists in the literature over the involvement of the endoplasmic reticulum (ER) in the delivery of membrane proteins to peroxisomes. In this study, the involvement of the ER in the trafficking of two Arabidopsis (Arabidopsis thaliana) peroxisomal membrane proteins was investigated using confocal laser scanning microscopy of living cells expressing fusions between enhanced yellow fluorescent protein (eYFP) and AtPEX2 and AtPEX10. The fusion proteins were always detected in peroxisomes and cytosol irrespective of the location of the eYFP tag or the level of expression. The cytosolic fluorescence was not due to cleavage of the eYFP reporter from the C-terminal fusion proteins. Blocking known ER transport routes using the fungal metabolite Brefeldin A or expressing dominant negative mutants of Sar1 or RabD2a had no effect on the trafficking of AtPEX2 and AtPEX10 to peroxisomes. We conclude that AtPEX2 and AtPEX10 are inserted into peroxisome membranes directly from the cytosol.
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