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Roos, J., Kelly, R.B. (1998). Dap160, a neural-specific eps15 homology and multiple SH3 domain-containing protein that interacts with Drosophila dynamin.  J. Biol. Chem. 273(30): 19108--19119.
FlyBase ID
FBrf0103356
Publication Type
Research paper
Abstract
The discovery of overlapping hot spots of dynamin (Estes, P. S., Roos, J., van der Bliek, A., Kelly, R. B., Krishnan, K. S., and Ramaswami, M. (1996) J. Neurosci. 16, 5443-5456) and the heterotetrameric adaptor 2 complex (Gonzalez-Gaitan, M., and J├Ąckle, H. (1997) Cell 88, 767-776) in Drosophila nerve terminals led to the concept of zones of active endocytosis close to sites of active exocytosis. The proline-rich domain of Drosophila dynamin was used to identify and purify a third component of the endocytosis zones. Dap160 (dynamin-associated protein 160 kDa) is a membrane-associated, dynamin-binding protein of 160 kDa that has four putative src homology 3 domains and an Eps15 homology domain, motifs frequently found in proteins associated with endocytosis. The binding capacities of the four putative src homology 3 domains were examined individually and in combination and shown to bind known proteins that contained proline-rich domains. Each binding site, however, was different in its preference for binding partners. We suggest that Dap160 is a scaffolding protein that helps anchor proteins required for endocytosis at sites where they are needed in the Drosophila nerve terminal.
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    Language of Publication
    English
    Additional Languages of Abstract
    Parent Publication
    Publication Type
    Journal
    Abbreviation
    J. Biol. Chem.
    Title
    Journal of Biological Chemistry
    Publication Year
    1905-
    ISBN/ISSN
    0021-9258
    Data From Reference
    Alleles (1)
    Genes (6)
    Physical Interactions (6)