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A more recent version of this article appeared on June 1, 2002
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Submitted on December 19, 2001
Revised on February 21, 2002
Accepted on March 18, 2002
1 Howard Hughes Medical Institute, Departments of Medicine, Microbiology, and Immunology, University of California at San Francisco, California 94143-0703; and Max-Planck-Institute for Molecular Physiology, Department of Physical Biochemistry, 44227 Dortmund, Germany
2 Institute for Hygiene, Department of Virology, University of Heidelberg, 69120 Heidelberg, Germany
3 Howard Hughes Medical Institute, Departments of Medicine, Microbiology, and Immunology, University of California at San Francisco, California 94143-0703
* Corresponding author. E-mail address: geyer{at}mpimf-heidelberg.mpg.de.
* Corresponding author. E-mail address: matija{at}itsa.ucsf.edu.
The vacuolar ATPase (V-ATPase) is a multisubunit enzyme that facilitates the acidification of intracellular compartments in eukaryotic cells and plays an important role in receptor-mediated endocytosis, intracellular trafficking processes and protein degradation. In this study we show that the C-terminal fragment of 350 residues of the regulatory subunit H (V1H) of the V-ATPase shares structural and functional homologies with the ß-chains of adaptor protein complexes. Moreover, the fragment is similar to a region in the ß-subunit of COPI coatomer complexes, which suggests the existence of a shared domain in these three different families of proteins. For ß-adaptins, this fragment binds to cytoplasmic di-leucine-based sorting motifs such as in HIV-1 Nef that mediate endocytic trafficking. Expression of this fragment in cells blocks the internalization of transmembrane proteins which depend on di-leucine-based motifs, while mutation of the consensus sequence GEY only partly diminishes the recognition of the sorting motif. Based on recent structural analysis, our results suggest that the di-leucine-binding domain consists of a HEAT or ARM repeat protein fold.
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