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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

A variety of physiological functions of phosphoinositide-binding proteins. Phosphatidylinositol (4, 5) bis-phosphate generates two second messengers, inositol (1, 4, 5) tris-phosphate(IP3) and diacylglycerol. In addition, phosphoinositides are involved in the regulation of actin binding proteins (1), various protein activities (2), endocytosis (3), membrane protrusions such as filopodia and lamellipodia (4) and the activities of N-WASP/WAVE proteins (5).
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Related In: Results  -  Collection


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fig01: A variety of physiological functions of phosphoinositide-binding proteins. Phosphatidylinositol (4, 5) bis-phosphate generates two second messengers, inositol (1, 4, 5) tris-phosphate(IP3) and diacylglycerol. In addition, phosphoinositides are involved in the regulation of actin binding proteins (1), various protein activities (2), endocytosis (3), membrane protrusions such as filopodia and lamellipodia (4) and the activities of N-WASP/WAVE proteins (5).

Mentions: To understand this review more easily, molecular interactions of phosphoinositide-binding proteins are summarized in Fig. 1.


Phosphoinositide-binding interface proteins involved in shaping cell membranes.

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

A variety of physiological functions of phosphoinositide-binding proteins. Phosphatidylinositol (4, 5) bis-phosphate generates two second messengers, inositol (1, 4, 5) tris-phosphate(IP3) and diacylglycerol. In addition, phosphoinositides are involved in the regulation of actin binding proteins (1), various protein activities (2), endocytosis (3), membrane protrusions such as filopodia and lamellipodia (4) and the activities of N-WASP/WAVE proteins (5).
© Copyright Policy - open-access
Related In: Results  -  Collection

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

fig01: A variety of physiological functions of phosphoinositide-binding proteins. Phosphatidylinositol (4, 5) bis-phosphate generates two second messengers, inositol (1, 4, 5) tris-phosphate(IP3) and diacylglycerol. In addition, phosphoinositides are involved in the regulation of actin binding proteins (1), various protein activities (2), endocytosis (3), membrane protrusions such as filopodia and lamellipodia (4) and the activities of N-WASP/WAVE proteins (5).
Mentions: To understand this review more easily, molecular interactions of phosphoinositide-binding proteins are summarized in Fig. 1.

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