Identification of phosphorylation sites in the mouse oestrogen receptor

被引：32

作者：

Lahooti, H ^{[1
]}

White, R ^{[1
]}

Hoare, SA ^{[1
]}

Rahman, D ^{[1
]}

Pappin, DJC ^{[1
]}

Parker, MG ^{[1
]}

机构：

[1] IMPERIAL CANC RES FUND, MOLEC ENDOCRINOL & PROT SEQUENCING LABS, LONDON WC2A 3PX, ENGLAND

来源：

JOURNAL OF STEROID BIOCHEMISTRY AND MOLECULAR BIOLOGY | 1995年 / 55卷 / 3-4期

关键词：

D O I：

10.1016/0960-0760(95)00188-3

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：

Phosphorylation sites in the mouse oestrogen receptor, expressed in COS-1 cells in the presence of 17 beta-oestradiol, have been mapped by solid phase microsequencing. The receptor was first radiolabelled with [P-32] orthophosphate and a number of H-3- or C-14-labelled amino acids, immunopurified and then tryptic peptides were separated by thin layer chromatography or high performance liquid chromatography. Amino acid sequence analysis indicated that Ser-122, Ser-156, Ser-158 and Ser-298 were phosphorylated. The substitution of Ser-122 and Ser-298 with alanine had a negligible effect on the transcriptional activity of the receptor in transfected cells. However, a reduction of transcriptional activity was observed when Ser-122 was mutated in the context of mutations in a putative amphipathic a-helix involved in AF-2 activity. Thus a region of AF-1 that encompasses Ser-122 appears to interact with AF-2 in the full-length receptor.

引用

页码：305 / 313

页数：9

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