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

Yumi Yoshida, Masahiro Kinuta, Tadashi Abe, Shuang Liang, Kenta Araki, Ottavio Cremona, Gilbert Di Paolo, Yoshinori Moriyama, Tatsuji Yasuda, Pietro De Camilli, Kohji Takei

Research output: Contribution to journalArticle

89 Citations (Scopus)

Abstract

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.

Original languageEnglish
Pages (from-to)3483-3491
Number of pages9
JournalEMBO Journal
Volume23
Issue number17
DOIs
Publication statusPublished - Sep 1 2004

Fingerprint

Dynamins
Lipid bilayers
Lipid Bilayers
Liposomes
GTP Phosphohydrolases
Cytosol
Personnel Selection
Unilamellar Liposomes
Oligomerization
amphiphysin
Proline
Knockout Mice
Synapses
Brain
Chemical activation

Keywords

  • Amphiphysin
  • Dynamin
  • Endocytosis
  • GTPase
  • Liposome

ASJC Scopus subject areas

  • Genetics
  • Cell Biology

Cite this

The stimulatory action of amphiphysin on dynamin function is dependent on lipid bilayer curvature. / Yoshida, Yumi; Kinuta, Masahiro; Abe, Tadashi; Liang, Shuang; Araki, Kenta; Cremona, Ottavio; Di Paolo, Gilbert; Moriyama, Yoshinori; Yasuda, Tatsuji; De Camilli, Pietro; Takei, Kohji.

In: EMBO Journal, Vol. 23, No. 17, 01.09.2004, p. 3483-3491.

Research output: Contribution to journalArticle

Yoshida, Y, Kinuta, M, Abe, T, Liang, S, Araki, K, Cremona, O, Di Paolo, G, Moriyama, Y, Yasuda, T, De Camilli, P & Takei, K 2004, 'The stimulatory action of amphiphysin on dynamin function is dependent on lipid bilayer curvature', EMBO Journal, vol. 23, no. 17, pp. 3483-3491. https://doi.org/10.1038/sj.emboj.7600355
Yoshida, Yumi ; Kinuta, Masahiro ; Abe, Tadashi ; Liang, Shuang ; Araki, Kenta ; Cremona, Ottavio ; Di Paolo, Gilbert ; Moriyama, Yoshinori ; Yasuda, Tatsuji ; De Camilli, Pietro ; Takei, Kohji. / The stimulatory action of amphiphysin on dynamin function is dependent on lipid bilayer curvature. In: EMBO Journal. 2004 ; Vol. 23, No. 17. pp. 3483-3491.
@article{a387b61481ab464cb484f08f608a333c,
title = "The stimulatory action of amphiphysin on dynamin function is dependent on lipid bilayer curvature",
abstract = "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.",
keywords = "Amphiphysin, Dynamin, Endocytosis, GTPase, Liposome",
author = "Yumi Yoshida and Masahiro Kinuta and Tadashi Abe and Shuang Liang and Kenta Araki and Ottavio Cremona and {Di Paolo}, Gilbert and Yoshinori Moriyama and Tatsuji Yasuda and {De Camilli}, Pietro and Kohji Takei",
year = "2004",
month = "9",
day = "1",
doi = "10.1038/sj.emboj.7600355",
language = "English",
volume = "23",
pages = "3483--3491",
journal = "EMBO Journal",
issn = "0261-4189",
publisher = "Nature Publishing Group",
number = "17",

}

TY - JOUR

T1 - The stimulatory action of amphiphysin on dynamin function is dependent on lipid bilayer curvature

AU - Yoshida, Yumi

AU - Kinuta, Masahiro

AU - Abe, Tadashi

AU - Liang, Shuang

AU - Araki, Kenta

AU - Cremona, Ottavio

AU - Di Paolo, Gilbert

AU - Moriyama, Yoshinori

AU - Yasuda, Tatsuji

AU - De Camilli, Pietro

AU - Takei, Kohji

PY - 2004/9/1

Y1 - 2004/9/1

N2 - 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.

AB - 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.

KW - Amphiphysin

KW - Dynamin

KW - Endocytosis

KW - GTPase

KW - Liposome

UR - http://www.scopus.com/inward/record.url?scp=4644280545&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=4644280545&partnerID=8YFLogxK

U2 - 10.1038/sj.emboj.7600355

DO - 10.1038/sj.emboj.7600355

M3 - Article

C2 - 15318165

AN - SCOPUS:4644280545

VL - 23

SP - 3483

EP - 3491

JO - EMBO Journal

JF - EMBO Journal

SN - 0261-4189

IS - 17

ER -