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Cited by 176

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Serine 167 is the major estradiol-induced phosphorylation site on the human estrogen receptor

Arnold, S. F.·1994·Molecular Endocrinology

Abstract

Serine 167 has been identified by radiolabel and amino acid sequencing as the major estrogen-induced phosphorylation site on the human estrogen receptor (hER) from human MCF-7 mammary carcinoma cells. The phosphorylation of the hER on serine 167 was estrogen-dependent, increasing 4-fold upon estradiol treatment of MCF-7 cells and accounted for almost half of the total [32P]phosphate incorporated into the recombinant hER from Sf9 insect cells and the native hER from MCF-7 cells. Casein kinase II was found to phosphorylate the purified recombinant hER on serine 167 in vitro. In addition, estradiol binding enhanced by 2-fold the phosphorylation of the purified recombinant hER by casein kinase II in vitro. Western blot analysis and [32P]phosphate incorporation confirmed the presence of casein kinase II in Sf9 cells. These results demonstrate that the hER is phosphorylated on serine 167 by casein kinase II in a hormone-dependent manner.

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Metadata

Authors
Arnold, S. F.
Venue
Molecular Endocrinology
Published
1994-09-01
Volume
8
Issue
9
Pages
1208-1214
ISSN
0888-8809 (ISSN-L)
OpenAlex
W2010042688
Cited by
176
References
1
FWCI
5.10
Type
journal article
Language
en
Open access
closed

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CoChat. (2026). Citation check: Serine 167 is the major estradiol-induced phosphorylation site on the human estrogen receptor. https://app.cochat.ai/papers/10.1210/me.8.9.1208
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Arnold, S. F. (1994). Serine 167 is the major estradiol-induced phosphorylation site on the human estrogen receptor. Molecular Endocrinology. https://doi.org/10.1210/me.8.9.1208

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