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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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Proteins that contain the BAR, EFC/F-BAR, and IMD/I-BAR domains.
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fig02: Proteins that contain the BAR, EFC/F-BAR, and IMD/I-BAR domains.

Mentions: The Bin-Amphiphysin-Rvs167 (BAR) domain was originally found in the N-terminal region of highly conserved mammalian and yeast amphiphysins. Increasing numbers of BAR domain-containing proteins including amphiphysin, endophilin, nadrin, oligophrenin, arfaptin, sorting nexin, ASAP1, PICK1, APPL, and proteins of the centaurin subfamily have been found (Fig. 2). All BAR domains form homodimers and deform PI(4,5)P2-containing liposomes to membrane tubules in vitro.39) The structure of the BAR domain of amphiphysin was the first to be solved, and the protein was demonstrated to be important for membrane deformation. The BAR domain structure is a banana-shaped dimer in which the concave surface is positively charged (Fig. 3).39) The positively charged concave surface of the domain attaches to the negatively charged inner surface of the plasma membrane, mostly through PI(4,5)P2 and phosphatidylserine. Furthermore, BAR domains from endophilin and amphiphysin have hydrophobic amino acids on their concave surfaces or dimer ends.39–41) The hydrophobic amino acids on the concave surface are inserted into the membrane, thereby strengthening the interaction between the membrane and the BAR domain. The BAR domain of amphiphysin deforms the membrane into narrow tubular invaginations, which are considered to correspond to the location of amphiphysin function at the late stage of endocytic vesicle formation. The BAR domain of SNX9 is closely connected to the PX domain, but the BAR and PX domain units of SNX9 have broad phosphoinositide specificity.42)


Phosphoinositide-binding interface proteins involved in shaping cell membranes.

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

Proteins that contain the BAR, EFC/F-BAR, and IMD/I-BAR domains.
© Copyright Policy - open-access
Related In: Results  -  Collection

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

fig02: Proteins that contain the BAR, EFC/F-BAR, and IMD/I-BAR domains.
Mentions: The Bin-Amphiphysin-Rvs167 (BAR) domain was originally found in the N-terminal region of highly conserved mammalian and yeast amphiphysins. Increasing numbers of BAR domain-containing proteins including amphiphysin, endophilin, nadrin, oligophrenin, arfaptin, sorting nexin, ASAP1, PICK1, APPL, and proteins of the centaurin subfamily have been found (Fig. 2). All BAR domains form homodimers and deform PI(4,5)P2-containing liposomes to membrane tubules in vitro.39) The structure of the BAR domain of amphiphysin was the first to be solved, and the protein was demonstrated to be important for membrane deformation. The BAR domain structure is a banana-shaped dimer in which the concave surface is positively charged (Fig. 3).39) The positively charged concave surface of the domain attaches to the negatively charged inner surface of the plasma membrane, mostly through PI(4,5)P2 and phosphatidylserine. Furthermore, BAR domains from endophilin and amphiphysin have hydrophobic amino acids on their concave surfaces or dimer ends.39–41) The hydrophobic amino acids on the concave surface are inserted into the membrane, thereby strengthening the interaction between the membrane and the BAR domain. The BAR domain of amphiphysin deforms the membrane into narrow tubular invaginations, which are considered to correspond to the location of amphiphysin function at the late stage of endocytic vesicle formation. The BAR domain of SNX9 is closely connected to the PX domain, but the BAR and PX domain units of SNX9 have broad phosphoinositide specificity.42)

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