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Phosphoinositide-binding interface proteins involved in shaping cell membranes.

Takenawa T - Proc. Jpn. Acad., Ser. B, Phys. Biol. Sci. (2010)

Bottom Line: 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.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.

View Article: PubMed Central - PubMed

Affiliation: Laboratory of Lipid Biochemistry, Graduate School of Medicine, Kobe University, Hyogo, Japan. takenawa@med.kobe-u.ac.jp

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.

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Related in: MedlinePlus

Functional models of the BAR, EFC/F-BAR, or IMD/I-BAR-containing proteins and of WASP/WAVE proteins in inward or outward deformation of the membrane. A. Role of BAR, EFC/F-BAR, and N-WASP in endocytosis. B. Role of IRSp53 and WAVE in the formation of outward protrusion.
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fig05: Functional models of the BAR, EFC/F-BAR, or IMD/I-BAR-containing proteins and of WASP/WAVE proteins in inward or outward deformation of the membrane. A. Role of BAR, EFC/F-BAR, and N-WASP in endocytosis. B. Role of IRSp53 and WAVE in the formation of outward protrusion.

Mentions: In mammalian cells, a detailed analysis of the time course of protein recruitment to the clathrin-coated pit and subsequent internalization into cells was performed.47,86) N-WASP, the Arp2/3 complex, and FBP17 were maximally recruited to the clathrin-coated pit when the clathrin disappeared or was endocytosed from the membrane (Fig. 5). Interestingly, dynamin recruitment to clathrin was faster than that of N-WASP or the Arp2/3 complex and was maximal when the amount of clathrin reached its maximum.86) Dynamin recruitment should be faster than that of FBP17 because N-WASP and FBP17 are recruited simultaneously to the clathrin-coated pit.47) Moreover, the tubules induced by FBP17 were antagonized by the expression of dynamin, but this dynamin-mediated antagonism of tubulation was dependent on actin filaments,43) suggesting that the actin filaments mediated by N-WASP are essential for the dynamin-mediated fission of tubulated membranes or clathrin-coated pits. The yeast homolog of dynamin Vps1p interacts with the actin filament binding protein Sla1p and functions in actin cytoskeletal organization.87)


Phosphoinositide-binding interface proteins involved in shaping cell membranes.

Takenawa T - Proc. Jpn. Acad., Ser. B, Phys. Biol. Sci. (2010)

Functional models of the BAR, EFC/F-BAR, or IMD/I-BAR-containing proteins and of WASP/WAVE proteins in inward or outward deformation of the membrane. A. Role of BAR, EFC/F-BAR, and N-WASP in endocytosis. B. Role of IRSp53 and WAVE in the formation of outward protrusion.
© Copyright Policy - open-access
Related In: Results  -  Collection

Show All Figures
getmorefigures.php?uid=PMC3108299&req=5

fig05: Functional models of the BAR, EFC/F-BAR, or IMD/I-BAR-containing proteins and of WASP/WAVE proteins in inward or outward deformation of the membrane. A. Role of BAR, EFC/F-BAR, and N-WASP in endocytosis. B. Role of IRSp53 and WAVE in the formation of outward protrusion.
Mentions: In mammalian cells, a detailed analysis of the time course of protein recruitment to the clathrin-coated pit and subsequent internalization into cells was performed.47,86) N-WASP, the Arp2/3 complex, and FBP17 were maximally recruited to the clathrin-coated pit when the clathrin disappeared or was endocytosed from the membrane (Fig. 5). Interestingly, dynamin recruitment to clathrin was faster than that of N-WASP or the Arp2/3 complex and was maximal when the amount of clathrin reached its maximum.86) Dynamin recruitment should be faster than that of FBP17 because N-WASP and FBP17 are recruited simultaneously to the clathrin-coated pit.47) Moreover, the tubules induced by FBP17 were antagonized by the expression of dynamin, but this dynamin-mediated antagonism of tubulation was dependent on actin filaments,43) suggesting that the actin filaments mediated by N-WASP are essential for the dynamin-mediated fission of tubulated membranes or clathrin-coated pits. The yeast homolog of dynamin Vps1p interacts with the actin filament binding protein Sla1p and functions in actin cytoskeletal organization.87)

Bottom Line: 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.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.

View Article: PubMed Central - PubMed

Affiliation: Laboratory of Lipid Biochemistry, Graduate School of Medicine, Kobe University, Hyogo, Japan. takenawa@med.kobe-u.ac.jp

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.

Show MeSH
Related in: MedlinePlus