Abstract
Amphiphysin 1, an endocytic adaptor concentrated at synapses that couples clathrin-mediated endocytosis to dynamin-dependentfission, wasalsoshowntohavearegulatoryroleinactindynamics. Here, we report that amphiphysin 1 interacts with N-WASP and stimulates N-WASP- and Arp2/ 3-dependent actin polymerization. Both the Src homology 3 and the N-BAR domains are required for this stimulation. Acidic liposome-triggered, N-WASP-dependent actin polymerization is strongly impaired in brain cytosol of amphiphysin 1 knock-out mice. FRET-FLIM analysis of Sertoli cells, where endogenously expressed amphiphysin 1 colocalizes with N-WASP in peripheral ruffles, confirmed the association between the two proteins in vivo. This association undergoes regulation and is enhanced by stimulating phosphatidylserine receptors on the cell surface with phosphatidylserine- containing liposomes that trigger ruffle formation. These results indicate that actin regulation is a key function of amphiphysin 1 and that such function cooperates with the endocytic adaptor role and membrane shaping/curvature sensing properties of the protein during the endocytic reaction.
| Original language | English |
|---|---|
| Pages (from-to) | 34244-34256 |
| Number of pages | 13 |
| Journal | Journal of Biological Chemistry |
| Volume | 284 |
| Issue number | 49 |
| DOIs | |
| Publication status | Published - Dec 4 2009 |
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ASJC Scopus subject areas
- Biochemistry
- Cell Biology
- Molecular Biology
Cite this
Dynamic interaction of amphiphysin with N-WASP regulates actin assembly. / Yamada, Hiroshi; Padilla-Parra, Sergi; Park, Sun Joo; Itoh, Toshiki; Chaineau, Mathilde; Monaldi, Ilaria; Cremona, Ottavio; Benfenati, Fabio; De Camilli, Pietro; Coppey-Moisan, Maïté; Tramier, Marc; Galli, Thierry; Takei, Kohji.
In: Journal of Biological Chemistry, Vol. 284, No. 49, 04.12.2009, p. 34244-34256.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Dynamic interaction of amphiphysin with N-WASP regulates actin assembly
AU - Yamada, Hiroshi
AU - Padilla-Parra, Sergi
AU - Park, Sun Joo
AU - Itoh, Toshiki
AU - Chaineau, Mathilde
AU - Monaldi, Ilaria
AU - Cremona, Ottavio
AU - Benfenati, Fabio
AU - De Camilli, Pietro
AU - Coppey-Moisan, Maïté
AU - Tramier, Marc
AU - Galli, Thierry
AU - Takei, Kohji
PY - 2009/12/4
Y1 - 2009/12/4
N2 - Amphiphysin 1, an endocytic adaptor concentrated at synapses that couples clathrin-mediated endocytosis to dynamin-dependentfission, wasalsoshowntohavearegulatoryroleinactindynamics. Here, we report that amphiphysin 1 interacts with N-WASP and stimulates N-WASP- and Arp2/ 3-dependent actin polymerization. Both the Src homology 3 and the N-BAR domains are required for this stimulation. Acidic liposome-triggered, N-WASP-dependent actin polymerization is strongly impaired in brain cytosol of amphiphysin 1 knock-out mice. FRET-FLIM analysis of Sertoli cells, where endogenously expressed amphiphysin 1 colocalizes with N-WASP in peripheral ruffles, confirmed the association between the two proteins in vivo. This association undergoes regulation and is enhanced by stimulating phosphatidylserine receptors on the cell surface with phosphatidylserine- containing liposomes that trigger ruffle formation. These results indicate that actin regulation is a key function of amphiphysin 1 and that such function cooperates with the endocytic adaptor role and membrane shaping/curvature sensing properties of the protein during the endocytic reaction.
AB - Amphiphysin 1, an endocytic adaptor concentrated at synapses that couples clathrin-mediated endocytosis to dynamin-dependentfission, wasalsoshowntohavearegulatoryroleinactindynamics. Here, we report that amphiphysin 1 interacts with N-WASP and stimulates N-WASP- and Arp2/ 3-dependent actin polymerization. Both the Src homology 3 and the N-BAR domains are required for this stimulation. Acidic liposome-triggered, N-WASP-dependent actin polymerization is strongly impaired in brain cytosol of amphiphysin 1 knock-out mice. FRET-FLIM analysis of Sertoli cells, where endogenously expressed amphiphysin 1 colocalizes with N-WASP in peripheral ruffles, confirmed the association between the two proteins in vivo. This association undergoes regulation and is enhanced by stimulating phosphatidylserine receptors on the cell surface with phosphatidylserine- containing liposomes that trigger ruffle formation. These results indicate that actin regulation is a key function of amphiphysin 1 and that such function cooperates with the endocytic adaptor role and membrane shaping/curvature sensing properties of the protein during the endocytic reaction.
UR - http://www.scopus.com/inward/record.url?scp=71749083025&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=71749083025&partnerID=8YFLogxK
U2 - 10.1074/jbc.M109.064204
DO - 10.1074/jbc.M109.064204
M3 - Article
C2 - 19759398
AN - SCOPUS:71749083025
VL - 284
SP - 34244
EP - 34256
JO - Journal of Biological Chemistry
JF - Journal of Biological Chemistry
SN - 0021-9258
IS - 49
ER -