TY - JOUR
T1 - Functional partnership between amphiphysin and dynamin in clathrin-mediated endocytosis
AU - Takei, Kohji
AU - Slepnev, Vladimir I.
AU - Haucke, Volker
AU - De Camilli, Pietro
N1 - Funding Information:
This work was supported in part by grants from the NIH and the US Army Medical Research and Development Command (to P.D.C.), and a long-term fellowship from the Human Frontier Science Program (to V.H.). Correspondence and requests for materials should be addressed to P.D.C.
PY - 1999/5
Y1 - 1999/5
N2 - Amphiphysin, a protein that is highly concentrated in nerve terminals, has been proposed to function as a linker between the clathrin coat and dynamin in the endocytosis of synaptic vesicles. Here, using a cell-free system, we provide direct morphological evidence in support of this hypothesis. Unexpectedly, we also find that amphiphysin-1, like dynamin-1, can transform spherical liposomes into narrow tubules. Moreover, amphiphysin-1 assembles with dynamin-1 into ring-like structures around the tubules and enhances the liposome-fragmenting activity of dynamin-1 in the presence of GTP. These results show that amphiphysin binds lipid bilayers, indicate a potential function for amphiphysin in the changes in bilayer curvature that accompany vesicle budding, and imply a close functional partnership between amphiphysin and dynamin in endocytosis.
AB - Amphiphysin, a protein that is highly concentrated in nerve terminals, has been proposed to function as a linker between the clathrin coat and dynamin in the endocytosis of synaptic vesicles. Here, using a cell-free system, we provide direct morphological evidence in support of this hypothesis. Unexpectedly, we also find that amphiphysin-1, like dynamin-1, can transform spherical liposomes into narrow tubules. Moreover, amphiphysin-1 assembles with dynamin-1 into ring-like structures around the tubules and enhances the liposome-fragmenting activity of dynamin-1 in the presence of GTP. These results show that amphiphysin binds lipid bilayers, indicate a potential function for amphiphysin in the changes in bilayer curvature that accompany vesicle budding, and imply a close functional partnership between amphiphysin and dynamin in endocytosis.
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U2 - 10.1038/9004
DO - 10.1038/9004
M3 - Article
C2 - 10559861
AN - SCOPUS:0033130119
SN - 1465-7392
VL - 1
SP - 33
EP - 39
JO - Nature Cell Biology
JF - Nature Cell Biology
IS - 1
ER -