Abstract
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.
Copyright 2010 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Adaptor Proteins, Signal Transducing / chemistry*
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Adaptor Proteins, Signal Transducing / genetics
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Adaptor Proteins, Signal Transducing / metabolism*
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Amino Acid Motifs / genetics
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Amino Acid Motifs / physiology
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Amino Acids, Basic / analysis*
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Amino Acids, Basic / chemistry
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Amino Acids, Basic / genetics
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Amino Acids, Basic / metabolism
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Cell Surface Extensions / genetics
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Cell Surface Extensions / metabolism*
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Crystallography, X-Ray
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Endocytosis / genetics
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HeLa Cells
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Humans
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Microtubules / chemistry
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Microtubules / genetics
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Microtubules / metabolism*
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Models, Biological
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Models, Molecular
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Mutant Proteins / chemistry
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Mutant Proteins / metabolism
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Peptide Mapping / methods
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Protein Structure, Tertiary
Substances
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Adaptor Proteins, Signal Transducing
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Amino Acids, Basic
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Mutant Proteins
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PACSIN2 protein, human