FEBS Lett 1997,
PMID: 9280305
McMahon, H T; Wigge, P; Smith, C
Amphiphysin is an SH3 domain protein that has been implicated in synaptic vesicle endocytosis. We have recently cloned a second amphiphysin isoform, Amph2 (sequence submitted to GenBank, Y13380). Proteins capable of forming a complex with amphiphysin were isolated from rat brain by using recombinant GST-Amph2 for binding experiments. As well as interacting with dynamin I, the full-length protein bound to a weaker 180-kDa band. Immunoblotting demonstrated this protein to be clathrin. To address whether this is a direct interaction, the clathrin binding to amphiphysin was reconstituted in vitro with purified proteins. The N-terminal domain of Amph2 is sufficient for clathrin binding. Dynamin, which interacts with the SH3 domain of Amph2, displaces clathrin from the N-terminus. We propose a model that may explain how clathrin and dynamin are recruited to non-overlapping sites of the coated pit.
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Text Mining Data
Dashed line = No text mining data
Manually curated Databases
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IRef Biogrid Interaction:
AP2A2
—
AMPH
(direct interaction, pull down)
-
IRef Biogrid Interaction:
AP1B1
—
AMPH
(direct interaction, pull down)
-
IRef Biogrid Interaction:
CLTC
—
AP1B1
(direct interaction, pull down)
-
IRef Biogrid Interaction:
DNM1
—
AMPH
(direct interaction, pull down)
-
IRef Biogrid Interaction:
CLTC
—
AP2A2
(direct interaction, pull down)
-
IRef Hprd Interaction:
BIN1
—
DNM1
(in vivo)
-
IRef Hprd Interaction:
BIN1
—
DNM1
(in vitro)
-
IRef Hprd Interaction:
BIN1
—
AP2A1
(in vitro)
-
IRef Hprd Interaction:
CLTC
—
AMPH
(in vitro)
-
IRef Hprd Interaction:
CLTC
—
AMPH
(in vivo)
In total, 8 gene pairs are associated to this article in curated databases