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J. Biol. Chem., Vol. 279, Issue 20, 21334-21342, May 14, 2004

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The Proteasome -Subunit XAPC7 Interacts Specifically with Rab7 and Late Endosomes^*

Jianbo Dong, Wei Chen, Angela Welford, and Angela Wandinger-Ness¶

From the Molecular Trafficking Laboratory, Department of Pathology, University of New Mexico School of Medicine, Albuquerque, New Mexico 87131

Rab7 is a key regulatory protein governing early to late endocytic membrane transport. In this study the proteasome -subunit XAPC7 (also known as PSMA7, RC6-1, and HSPC in mammals) was identified to interact specifically with Rab7 and was recruited to multivesicular late endosomes through this interaction. The protein interaction domains were localized to the C terminus of XAPC7 and the N terminus of Rab7. XAPC7 was not found on early or recycling endosomes, but could be recruited to recycling endosomes by expression of a Rab7-(1-174)Rab11-(160-202) chimera, establishing a central role for Rab7 in the membrane recruitment of XAPC7. Although XAPC7 could be shown to associate with membranes bearing ubiquitinated cargo, overexpression had no impact on steady-state ubiquitinated protein levels. Most notably, overexpression of XAPC7 was found to impair late endocytic transport of two different membrane proteins, including EGFR known to be highly dependent on ubiquitination and proteasome activity for proper endocytic sorting and lysosomal transport. Decreased late endocytic transport caused by XAPC7 overexpression was partially rescued by coexpression of wild-type Rab7, suggesting a negative regulatory role for XAPC7. Nevertheless, Rab7 itself was not subject to XAPC7-dependent proteasomal degradation. Together the data establish the first direct molecular link between the endocytic trafficking and cytosolic degradative machineries.

Received for publication, January 29, 2004 , and in revised form, March 2, 2004.

^* This work was supported by the National Science Foundation (MCB9982161). 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 nucleotide sequence(s) reported in this paper has been submitted to the GenBank^TM/EBI Data Bank with accession number(s) AY526609.

Current address: Center for Biotechnology and Genomic Medicine, Medical College of Georgia, Augusta, GA 30912.

^¶ To whom correspondence should be addressed: University of New Mexico HSC, 2325 Camino de Salud NE, CRF 225, Albuquerque, New Mexico 87131. Tel.: 505-272-1459; Fax: 505-272-4193; E-mail: wness{at}unm.edu.

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