Biochemical and functional significance of F-BAR domain proteins interaction with WASP/N-WASP

被引：14

作者：

Chen, Yolande ^{[1
,2
]}

Aardema, Jorie ^{[1
,2
]}

Corey, Seth J. ^{[1
,2
]}

机构：

[1] Northwestern Univ, Feinberg Sch Med, Dept Pediat, Chicago, IL 60611 USA

[2] Northwestern Univ, Feinberg Sch Med, Dept Cell & Mol Biol, Chicago, IL 60611 USA

来源：

SEMINARS IN CELL & DEVELOPMENTAL BIOLOGY | 2013年 / 24卷 / 04期

基金：

美国国家卫生研究院;

关键词：

BAR proteins; Wiskott-Aldrich Syndrome Protein; Actin; Membrane remodeling; WISKOTT-ALDRICH-SYNDROME; X-LINKED NEUTROPENIA; N-WASP; ACTIN POLYMERIZATION; MEMBRANE INVAGINATION; CONGENITAL NEUTROPENIA; PROPLATELET FORMATION; MENTAL-RETARDATION; STRUCTURAL BASIS; FAMILY PROTEINS;

D O I：

10.1016/j.semcdb.2013.01.005

中图分类号：

Q2 [细胞生物学];

学科分类号：

071013 [干细胞生物学];

摘要：

The Bin-Amphiphysin-Rvs (BAR) domain family of proteins includes groups which promote positive (classical BAR, N-BAR, and F-BAR) and negative (I-BAR) membrane deformation. Of these groups, the F-BAR subfamily is the most diverse in its biochemical properties. F-BAR domain proteins dimerize to form a tight scaffold about the membrane. The F-BAR domain provides a banana-shaped, alpha-helical structure that senses membrane curvature. Different types of F-BAR domain proteins contain tyrosine kinase or GTPase activities; some interact with phosphatases and RhoGTPases. Most possess an SH3 domain that facilitates the recruitment and activation of WASP/N-WASP. Thus, F-BAR domain proteins affect remodeling of both membrane and the actin cytoskeleton. The purpose of this review is to highlight the role of F-BAR proteins in coupling WASP/N-WASP to cytoskeletal remodeling. A role for F-BAR/WASP interaction in human diseases affecting nervous, blood, and neoplastic tissues is discussed. (C) 2013 Published by Elsevier Ltd.

引用

收藏

页码：280 / 286

页数：7

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