Abstract
Caveolae are flask-shaped invaginations of the plasma membrane that are associated with tumor formation, pathogen entry and muscular dystrophy, through the regulation of lipids, signal transduction and endocytosis. Caveolae are generated by the fusion of caveolin-1-containing vesicles with the plasma membrane, which then participate in endocytosis via dynamin. Proteins containing membrane-sculpting F-BAR (or EFC) domains organize the membrane in clathrin-mediated endocytosis. Here, we show that the FBAR protein PACSIN2 sculpts the plasma membrane of the caveola. The PACSIN2 F-BAR domain interacts directly with caveolin-1 by unmasking autoinhibition of PACSIN2. Furthermore, the membrane invaginations induced by the PACSIN2 F-BAR domain contained caveolin-1. Knockdown of PACSIN2 resulted in abnormal morphology of caveolin-1-associated plasma membranes, presumably as a result of decreased recruitment of dynamin-2 to caveolin-1. These results indicate that PACSIN2 mediates membrane sculpting by caveolin-1 in caveola morphology and recruits dynamin-2 for caveola fission.
| Original language | English |
|---|---|
| Pages (from-to) | 2032-2040 |
| Number of pages | 9 |
| Journal | Journal of cell science |
| Volume | 124 |
| Issue number | 12 |
| DOIs | |
| Publication status | Published - Jun 15 2011 |
| Externally published | Yes |
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Keywords
- Caveolae
- EFC domain
- F-BAR domain
- Membrane sculpting
ASJC Scopus subject areas
- Cell Biology
Cite this
Essential role of PACSIN2/syndapin-II in caveolae membrane sculpting. / Senju, Yosuke; Itoh, Yuzuru; Takano, Kazunori; Hamada, Sayaka; Suetsugu, Shiro.
In: Journal of cell science, Vol. 124, No. 12, 15.06.2011, p. 2032-2040.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Essential role of PACSIN2/syndapin-II in caveolae membrane sculpting
AU - Senju, Yosuke
AU - Itoh, Yuzuru
AU - Takano, Kazunori
AU - Hamada, Sayaka
AU - Suetsugu, Shiro
PY - 2011/6/15
Y1 - 2011/6/15
N2 - Caveolae are flask-shaped invaginations of the plasma membrane that are associated with tumor formation, pathogen entry and muscular dystrophy, through the regulation of lipids, signal transduction and endocytosis. Caveolae are generated by the fusion of caveolin-1-containing vesicles with the plasma membrane, which then participate in endocytosis via dynamin. Proteins containing membrane-sculpting F-BAR (or EFC) domains organize the membrane in clathrin-mediated endocytosis. Here, we show that the FBAR protein PACSIN2 sculpts the plasma membrane of the caveola. The PACSIN2 F-BAR domain interacts directly with caveolin-1 by unmasking autoinhibition of PACSIN2. Furthermore, the membrane invaginations induced by the PACSIN2 F-BAR domain contained caveolin-1. Knockdown of PACSIN2 resulted in abnormal morphology of caveolin-1-associated plasma membranes, presumably as a result of decreased recruitment of dynamin-2 to caveolin-1. These results indicate that PACSIN2 mediates membrane sculpting by caveolin-1 in caveola morphology and recruits dynamin-2 for caveola fission.
AB - Caveolae are flask-shaped invaginations of the plasma membrane that are associated with tumor formation, pathogen entry and muscular dystrophy, through the regulation of lipids, signal transduction and endocytosis. Caveolae are generated by the fusion of caveolin-1-containing vesicles with the plasma membrane, which then participate in endocytosis via dynamin. Proteins containing membrane-sculpting F-BAR (or EFC) domains organize the membrane in clathrin-mediated endocytosis. Here, we show that the FBAR protein PACSIN2 sculpts the plasma membrane of the caveola. The PACSIN2 F-BAR domain interacts directly with caveolin-1 by unmasking autoinhibition of PACSIN2. Furthermore, the membrane invaginations induced by the PACSIN2 F-BAR domain contained caveolin-1. Knockdown of PACSIN2 resulted in abnormal morphology of caveolin-1-associated plasma membranes, presumably as a result of decreased recruitment of dynamin-2 to caveolin-1. These results indicate that PACSIN2 mediates membrane sculpting by caveolin-1 in caveola morphology and recruits dynamin-2 for caveola fission.
KW - Caveolae
KW - EFC domain
KW - F-BAR domain
KW - Membrane sculpting
UR - http://www.scopus.com/inward/record.url?scp=79958105143&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=79958105143&partnerID=8YFLogxK
U2 - 10.1242/jcs.086264
DO - 10.1242/jcs.086264
M3 - Article
C2 - 21610094
AN - SCOPUS:79958105143
VL - 124
SP - 2032
EP - 2040
JO - Journal of Cell Science
JF - Journal of Cell Science
SN - 0021-9533
IS - 12
ER -