TY - JOUR
T1 - Mapping of the basic amino-acid residues responsible for tubulation and cellular protrusion by the EFC/F-BAR domain of pacsin2/Syndapin II
AU - Shimada, Atsushi
AU - Takano, Kazunori
AU - Shirouzu, Mikako
AU - Hanawa-Suetsugu, Kyoko
AU - Terada, Takaho
AU - Toyooka, Kiminori
AU - Umehara, Takashi
AU - Yamamoto, Masaki
AU - Yokoyama, Shigeyuki
AU - Suetsugu, Shiro
N1 - Funding Information:
We thank Noboru Ohsawa, Ayako Sakamoto, Mio Inoue, Aki Makanae, Yoshiko Ishizuka-Katsura, Yuri Tomabechi, Tomomi Uchikubo-Kamo, and Ryogo Akasaka for sample preparation. We thank Hideaki Niwa and Takashi Wada for X-ray diffraction data collection. We thank the beamline staffs at BL-5A at Photon Factory (Tsukuba, Japan) and BL26B2 and BL41XU at SPring-8 (Hyogo, Japan) for assistance with our X-ray data collection. This work was supported in part by a Grant-in-Aid from the Ministry of Education, Culture, Sports, Science and Technology of Japan (to A.S. and S.S.), Grants-in-Aid from the Japan Science and Technology Corporation (JST) (to S.S.), the Ono Medical Research Foundation (to S.S.), the Mochida Memorial Foundation for Medical and Pharmaceutical Research (to S.S.), the Takeda Science Foundation (to S.S.), and the Targeted Proteins Research Program (TPRP) from Ministry of Education, Culture, Sports, Science and Technology of Japan .
PY - 2010/3
Y1 - 2010/3
N2 - The extended Fes-CIP4 homology (EFC)/FCH-BAR (F-BAR) domain tubulates membranes. Overexpression of the pacsin2 EFC/F-BAR domain resulted in tubular localization inside cells and deformed liposomes into tubules in vitro. We found that overexpression of the pacsin2 EFC/F-BAR domain induced cellular microspikes, with the pacsin2 EFC/F-BAR domain concentrated at the neck. The hydrophobic loops and the basic amino-acid residues on the concave surface of the pacsin2 EFC/F-BAR domain are essential for both the microspike formation and tubulation. Since the curvature of the neck of the microspike and that of the tubulation share similar geometry, the pacsin2 EFC/F-BAR domain is considered to facilitate both microspike formation and tubulation.
AB - The extended Fes-CIP4 homology (EFC)/FCH-BAR (F-BAR) domain tubulates membranes. Overexpression of the pacsin2 EFC/F-BAR domain resulted in tubular localization inside cells and deformed liposomes into tubules in vitro. We found that overexpression of the pacsin2 EFC/F-BAR domain induced cellular microspikes, with the pacsin2 EFC/F-BAR domain concentrated at the neck. The hydrophobic loops and the basic amino-acid residues on the concave surface of the pacsin2 EFC/F-BAR domain are essential for both the microspike formation and tubulation. Since the curvature of the neck of the microspike and that of the tubulation share similar geometry, the pacsin2 EFC/F-BAR domain is considered to facilitate both microspike formation and tubulation.
UR - http://www.scopus.com/inward/record.url?scp=77950368868&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=77950368868&partnerID=8YFLogxK
U2 - 10.1016/j.febslet.2010.02.058
DO - 10.1016/j.febslet.2010.02.058
M3 - Article
C2 - 20188097
AN - SCOPUS:77950368868
VL - 584
SP - 1111
EP - 1118
JO - FEBS Letters
JF - FEBS Letters
SN - 0014-5793
IS - 6
ER -