期刊
PROCEEDINGS OF THE JAPAN ACADEMY SERIES B-PHYSICAL AND BIOLOGICAL SCIENCES
卷 86, 期 5, 页码 509-523出版社
JAPAN ACAD
DOI: 10.2183/pjab.86.509
关键词
phosphoinositide; membrane-deforming proteins; N-WASP; WAVE; BAR domain; F-BAR domain
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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