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Subunit H of the V-ATPase Involved in Endocytosis Shows Homology to β-Adaptins

MPG-Autoren
http://pubman.mpdl.mpg.de/cone/persons/resource/persons98692

Geyer,  Matthias
Abt. III: Physikalische Biochemie, Max Planck Institute of Molecular Physiology, Max Planck Society;

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Zitation

Geyer, M., Fackler, O. T., & Peterlin, B. M. (2002). Subunit H of the V-ATPase Involved in Endocytosis Shows Homology to β-Adaptins. Molecular Biology of the Cell, 13(6): 1, pp. 2045-2056. Retrieved from http://www.molbiolcell.org/cgi/content/abstract/13/6/2045.


Zitierlink: http://hdl.handle.net/11858/00-001M-0000-0014-0E60-3
Zusammenfassung
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 beta-chains of adaptor protein complexes. Moreover, the fragment is similar to a region in the beta-subunit of COPI coatomer complexes, which suggests the existence of a shared domain in these three different families of proteins. For beta- 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.