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Vol. 8, Issue 10, 2003-2015, October 1997
The Neurobiology Division, Medical Research Council Laboratory of
Molecular Biology, Cambridge, CB2 2QH, United Kingdom
Amphiphysin (Amph) is a src homology 3 domain-containing
protein that has been implicated in synaptic vesicle endocytosis as a
result of its interaction with dynamin. In a screen for novel members
of the amphiphysin family, we identified Amph2, an isoform 49%
identical to the previously characterized Amph1 protein. The subcellular distribution of this isoform parallels Amph1, both being
enriched in nerve terminals. Like Amph1, a role in endocytosis at the
nerve terminal is supported by the rapid dephosphorylation of Amph2 on
depolarization. Importantly, the two isoforms can be
coimmunoprecipitated from the brain as an equimolar complex, suggesting
that the two isoforms act in concert. As determined by cross-linking of
brain extracts, the Amph1-Amph2 complex is a 220- to 250-kDa
heterodimer. COS cells transfected with either Amph1 or Amph2 show
greatly reduced transferrin uptake, but coexpression of the two
proteins rescues this defect, supporting a role for the heterodimer in
clathrin-mediated endocytosis. Although the src homology 3 domains of
both isoforms interact with dynamin, the heterodimer can associate with
multiple dynamin molecules in vitro and activates dynamin's GTPase
activity. We propose that it is an amphiphysin heterodimer that drives
the recruitment of dynamin to clathrin-coated pits in endocytosing
nerve terminals.
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