Phosphoinositide-binding interface proteins involved in shaping cell membranes

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  • TAKENAWA Tadaomi
    Laboratory of Lipid Biochemistry, Graduate School of Medicine, Kobe University

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  • Phosphoinositede-binding interface proteins involved in the shaping cell membrane

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Abstract

The mechanism by which cell and cell membrane shapes are created has long been a subject of great interest. Among the phosphoinositide-binding proteins, a group of proteins that can change the shape of membranes, in addition to the phosphoinositide-binding ability, has been found. These proteins, which contain membrane-deforming domains such as the BAR, EFC/F-BAR, and the IMD/I-BAR domains, led to inward-invaginated tubes or outward protrusions of the membrane, resulting in a variety of membrane shapes. Furthermore, these proteins not only bind to phosphoinositide, but also to the N-WASP/WAVE complex and the actin polymerization machinery, which generates a driving force to shape the membranes.<BR><BR>(Communicated by Takao SEKIYA, M.J.A.)

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