DEP domains: structurally similar but functionally different

被引：60
作者：
Consonni, Sarah V. [1 ]
Maurice, Madelon M. [2 ]
Bos, Johannes L. [1 ]
机构：
[1] Univ Med Ctr Utrecht, Ctr Mol Med, NL-3584 CG Utrecht, Netherlands
[2] Univ Med Ctr Utrecht, Ctr Mol Med, Dept Cell Biol, NL-3584 CX Utrecht, Netherlands
来源：
NATURE REVIEWS MOLECULAR CELL BIOLOGY | 2014年 / 15卷 / 05期
关键词：
PLANAR CELL POLARITY; EXCHANGE FACTOR EPAC2; CYCLIC-AMP; PROTEINS; MEMBRANE; P-REX1; REGULATORS; FAMILY; RGS; PHOSPHORYLATION;
D O I：
10.1038/nrm3791
中图分类号：
Q2 [细胞生物学];
学科分类号：
071009 ; 090102 ;
摘要：
The Dishevelled, EGL-10 and pleckstrin (DEP) domain is a globular protein domain that is present in about ten human protein families with well-defined structural features. A picture is emerging that DEP domains mainly function in the spatial and temporal control of diverse signal transduction events by recruiting proteins to the plasma membrane. DEP domains can interact with various partners at the membrane, including phospholipids and membrane receptors, and their binding is subject to regulation.
引用
收藏
页码：357 / 362
页数：6
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