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J. Biol. Chem., Vol. 280, Issue 48, 40135-40143, December 2, 2005

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The DnaJ-domain Protein RME-8 Functions in Endosomal Trafficking^*

From the Department of Neurology and Neurosurgery, Montreal Neurological Institute, McGill University, Montreal QC H3A 2B4, Canada

Through a proteomic analysis of clathrin-coated vesicles from rat liver we identified the mammalian homolog of receptor-mediated endocytosis 8 (RME-8), a DnaJ domain-containing protein originally identified in a screen for endocytic defects in Caenorhabditis elegans. Mammalian RME-8 has a broad tissue distribution, and affinity selection assays reveal the ubiquitous chaperone Hsc70, which regulates protein conformation at diverse membrane sites as the major binding partner for its DnaJ domain. RME-8 is tightly associated with microsomal membranes and co-localizes with markers of the endosomal system. Small interfering RNA-mediated knock down of RME-8 has no influence on transferrin endocytosis but causes a reduction in epidermal growth factor internalization. Interestingly, and consistent with a localization to endosomes, knock down of RME-8 also leads to alterations in the trafficking of the cation-independent mannose 6-phosphate receptor and improper sorting of the lysosomal hydrolase cathepsin D. Our data demonstrate that RME-8 functions in intracellular trafficking and provides the first evidence of a functional role for a DnaJ domain-bearing co-chaperone on endosomes.

Received for publication, May 6, 2005 , and in revised form, September 16, 2005.

The nucleotide sequence(s) reported in this paper has been submitted to the GenBank^TM/EBI Data Bank with accession number(s) AY779857 [GenBank] .

^* This work was supported by Canadian Institutes of Health Research Grant MOP-105863 (to P. S. M.). Operating grants from the Genome Quebec/Genome Canada project Réseau Protéomique de Montréal, Montreal Proteomics Network also supported this work. The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

The on-line version of this article (available at http://www.jbc.org) contains Supplemental Figs. 1 and 2.

¹ These authors are equal contributors.

² Recipient of a Canadian Institutes of Health Research studentship.

³ Recipient of a Canadian Institutes of Health Research fellowship.

⁴ To whom correspondence should be addressed: Dept. of Neurology and Neurosurgery, Montreal Neurological Institute, McGill University, 3801 University St., Montreal, QC H3A 2B4. Tel.: 514-398-7355; Fax: 514-398-8106; E-mail: peter.mcpherson{at}mcgill.ca.

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