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Roles of NHERF1/EBP50 in cancer
被引:87
作者:

Georgescu, Maria-Magdalena
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机构:
Univ Texas MD Anderson Canc Ctr, Dept Neurooncol, Houston, TX 77030 USA Univ Texas MD Anderson Canc Ctr, Dept Neurooncol, Houston, TX 77030 USA

Morales, Fabiana C.
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Univ Texas MD Anderson Canc Ctr, Dept Neurooncol, Houston, TX 77030 USA Univ Texas MD Anderson Canc Ctr, Dept Neurooncol, Houston, TX 77030 USA

Molina, Jennifer R.
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Univ Texas MD Anderson Canc Ctr, Dept Neurooncol, Houston, TX 77030 USA Univ Texas MD Anderson Canc Ctr, Dept Neurooncol, Houston, TX 77030 USA

Hayashi, Yuho
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机构:
Univ Texas MD Anderson Canc Ctr, Dept Neurooncol, Houston, TX 77030 USA Univ Texas MD Anderson Canc Ctr, Dept Neurooncol, Houston, TX 77030 USA
机构:
[1] Univ Texas MD Anderson Canc Ctr, Dept Neurooncol, Houston, TX 77030 USA
关键词:
D O I:
10.2174/156652408785748031
中图分类号:
R-3 [医学研究方法];
R3 [基础医学];
学科分类号:
1001 ;
摘要:
This review summarizes the emerging roles of NHERF1/EBP50 adaptor protein in tumorigenesis. NHERF1/EBP50 ((N) under bara(+)/(H) under bar (+) (e) under bar xchanger (r) under bar egulating (f) under bar actor 1; ezrin-radixin-moesin ((E) under bar RM) (b) under bar inding (p) under bar hosphoprotein of 50 kDa) is a PDZ domain-containing protein with physiological localization at the plasma membrane. We discuss in this review the functions of NHERF1/EBP50 as a linker between membrane proteins and the cytoskeleton network, as well as its involvement in different types of cancer, such as breast and liver cancers. Recent evidence obtained from our laboratory and from other groups shows that NHERF1/EBP50 is an important player in cancer progression. It appears that, depending on its subcellular distribution, NHERF1/EBP50 may behave either as a tumor suppressor, when it is localized at the plasma membrane, or as an oncogenic protein, when it is shifted to the cytoplasm. We provide here an overview of the mechanisms by which this adaptor protein controls cell transformation, and propose a model suggesting a dual role of NHERF1/EBP50 in cancer.
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页码:459 / 468
页数:10
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