MISC

2004年9月

The stimulatory action of amphiphysin on dynamin function is dependent on lipid bilayer curvature

EMBO JOURNAL
  • Y Yoshida
  • ,
  • M Kinuta
  • ,
  • T Abe
  • ,
  • S Liang
  • ,
  • K Araki
  • ,
  • O Cremona
  • ,
  • G Di Paolo
  • ,
  • Y Moriyama
  • ,
  • T Yasuda
  • ,
  • P De Camilli
  • ,
  • K Takei

23
17
開始ページ
3483
終了ページ
3491
記述言語
英語
掲載種別
DOI
10.1038/sj.emboj.7600355
出版者・発行元
NATURE PUBLISHING GROUP

Amphiphysin is a major dynamin-binding partner at the synapse; however, its function in fission is unclear. Incubation of large unilamellar liposomes with mice brain cytosol led to massive formation of small vesicles, whereas cytosol of amphiphysin 1 knockout mice was much less efficient in this reaction. Vesicle formation from large liposomes by purified dynamin was also strongly enhanced by amphiphysin. In the presence of liposomes, amphiphysin strongly affected dynamin GTPase activity and the recruitment of dynamin to the liposomes, but this activity was highly dependent on liposome size. Deletion from amphiphysin of its central proline-rich stretch dramatically potentiated its effect on dynamin, possibly by relieving an inhibitory intramolecular interaction. These results suggest a model in which maturation of endocytic pits correlates with the oligomerization of dynamin with either amphiphysin or other proteins with similar domain structure. Formation of these complexes is coupled to the activation of dynamin GTPase activity, thus explaining how deep invagination of the pit leads to fission.


リンク情報
DOI
https://doi.org/10.1038/sj.emboj.7600355
Web of Science
https://gateway.webofknowledge.com/gateway/Gateway.cgi?GWVersion=2&SrcAuth=JSTA_CEL&SrcApp=J_Gate_JST&DestLinkType=FullRecord&KeyUT=WOS:000223732800005&DestApp=WOS_CPL
ID情報
  • DOI : 10.1038/sj.emboj.7600355
  • ISSN : 0261-4189
  • Web of Science ID : WOS:000223732800005

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