PMID- 10559861
OWN - NLM
STAT- MEDLINE
DCOM- 19991207
LR  - 20061115
IS  - 1465-7392 (Print)
IS  - 1465-7392 (Linking)
VI  - 1
IP  - 1
DP  - 1999 May
TI  - Functional partnership between amphiphysin and dynamin in clathrin-mediated
      endocytosis.
PG  - 33-9
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.
FAU - Takei, K
AU  - Takei K
AD  - Department of Cell Biology, Yale University School of Medicine, New Haven,
      Connecticut 06510, USA.
FAU - Slepnev, V I
AU  - Slepnev VI
FAU - Haucke, V
AU  - Haucke V
FAU - De Camilli, P
AU  - De Camilli P
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PT  - Research Support, U.S. Gov't, Non-P.H.S.
PT  - Research Support, U.S. Gov't, P.H.S.
PL  - England
TA  - Nat Cell Biol
JT  - Nature cell biology
JID - 100890575
RN  - 0 (Clathrin)
RN  - 0 (Liposomes)
RN  - 0 (Nerve Tissue Proteins)
RN  - 0 (Recombinant Proteins)
RN  - 147954-52-7 (amphiphysin)
RN  - EC 3.5.1.50 (Dynamin I)
RN  - EC 3.6.1.- (GTP Phosphohydrolases)
RN  - EC 3.6.5.5 (Dynamins)
SB  - IM
CIN - Nat Cell Biol. 1999 May;1(1):E8-9. PMID: 10559872
MH  - Animals
MH  - Brain/metabolism
MH  - Cattle
MH  - Cell-Free System
MH  - Clathrin/chemistry/*metabolism/ultrastructure
MH  - Coated Pits, Cell-Membrane/physiology/ultrastructure
MH  - Dimerization
MH  - Dynamin I
MH  - Dynamins
MH  - Endocytosis/*physiology
MH  - GTP Phosphohydrolases/chemistry/*metabolism/ultrastructure
MH  - Humans
MH  - Kinetics
MH  - Liposomes
MH  - Microscopy, Electron
MH  - Nerve Tissue Proteins/chemistry/*metabolism/ultrastructure
MH  - Recombinant Proteins/chemistry/metabolism/ultrastructure
EDAT- 1999/11/13 09:00
MHDA- 2001/03/23 10:01
CRDT- 1999/11/13 09:00
PHST- 1999/11/13 09:00 [pubmed]
PHST- 2001/03/23 10:01 [medline]
PHST- 1999/11/13 09:00 [entrez]
AID - 10.1038/9004 [doi]
PST - ppublish
SO  - Nat Cell Biol. 1999 May;1(1):33-9. doi: 10.1038/9004.