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Vol. 13, Issue 6, 2045-2056, June 2002
-Adaptins
*Howard Hughes Medical Institute, Departments of Medicine,
Microbiology, and Immunology, University of California at San
Francisco, California 94143-0703; 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 Max-Planck-Institute
for Molecular Physiology, Department of Physical Biochemistry, 44227 Dortmund, Germany; and §Institute for Hygiene, Department
of Virology, University of Heidelberg, 69120 Heidelberg, Germany
-chains of adaptor
protein complexes. Moreover, the fragment is similar to a region in the
-subunit of COPI coatomer complexes, which suggests the existence of
a shared domain in these three different families of proteins. For
-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,
whereas 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.
Corresponding authors. E-mail addresses:
geyer{at}mpimf-heidelberg.mpg.de and matija{at}itsa.ucsf.edu.
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