Mapping of the basic amino-acid residues responsible for tubulation and cellular protrusion by the EFC/F-BAR domain of pacsin2/Syndapin II.
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.
Shimada
Atsushi
A
RIKEN Systems and Structural Biology Center, Tsurumi, Yokohama, Japan.
Takano
Kazunori
K
Shirouzu
Mikako
M
Hanawa-Suetsugu
Kyoko
K
Terada
Takaho
T
Toyooka
Kiminori
K
Umehara
Takashi
T
Yamamoto
Masaki
M
Yokoyama
Shigeyuki
S
Suetsugu
Shiro
S
D048868:Adaptor Proteins, Signal Transducing / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*; D020816:Amino Acid Motifs / Q000235:genetics / Q000502:physiology; D024361:Amino Acids, Basic / Q000032:analysis* / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D022081:Cell Surface Extensions / Q000235:genetics / Q000378:metabolism*; D018360:Crystallography, X-Ray; D004705:Endocytosis / Q000235:genetics; D006367:HeLa Cells; D006801:Humans; D008870:Microtubules / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D008954:Models, Biological; D008958:Models, Molecular; D050505:Mutant Proteins / Q000737:chemistry / Q000378:metabolism; D010449:Peptide Mapping / Q000379:methods; D017434:Protein Structure, Tertiary
D048868:Adaptor Proteins, Signal Transducing; D024361:Amino Acids, Basic; D050505:Mutant Proteins; C120714:PACSIN2 protein, human