Estrogen receptor phosphorylation

被引:365
作者
Lannigan, DA [1 ]
机构
[1] Univ Virginia, Hlth Sci Ctr, Ctr Cell Signaling, Charlottesville, VA 22908 USA
关键词
estrogen receptor; phosphorylation; transcription;
D O I
10.1016/S0039-128X(02)00110-1
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Estrogen receptor alpha (ERalpha) is phosphorylated on multiple amino acid residues. For example, in response to estradiol binding, human ERalpha is predominately phosphorylated on Ser-118 and to a lesser extent on Ser-104 and Ser-106. In response to activation of the mitogen-activated protein kinase pathway, phosphorylation occurs on Ser-118 and Ser-167. These serine residues are all located within the activation function 1 region of the N-terminal domain of ERalpha. In contrast, activation of protein kinase A increases the phosphorylation of Ser-236, which is located in the DNA-binding domain. The in vivo phosphorylation status of Tyr-537, located in the ligand-binding domain, remains controversial. In this review, I present evidence that these phosphorylations occur, and identify the kinases thought to be responsible. Additionally, the functional importance of ERalpha phosphorylation is discussed. (C) 2002 Elsevier Science Inc. All rights reserved.
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页码:1 / 9
页数:9
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