Phosphoinositide-binding interface proteins involved in shaping cell membranes.
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.
Takenawa
Tadaomi
T
Laboratory of Lipid Biochemistry, Graduate School of Medicine, Kobe University, Hyogo, Japan. takenawa@med.kobe-u.ac.jp
D000818:Animals; D002462:Cell Membrane / Q000737:chemistry* / Q000378:metabolism*; D006801:Humans; D010716:Phosphatidylinositols / Q000378:metabolism*; D017434:Protein Structure, Tertiary; D011506:Proteins / Q000737:chemistry / Q000378:metabolism*
D010716:Phosphatidylinositols; D011506:Proteins
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