Unknown

Dataset Information

0

Phosphorylation of human estrogen receptor-beta at serine 105 inhibits breast cancer cell migration and invasion.


ABSTRACT: Multiple phosphorylation sites on the human estrogen receptor (hER)? were identified and shown to influence mammary carcinogenesis. In contrast, functional phosphorylation sites of hER? have yet to be experimentally identified and validated. Here, using mass spectrometry, we uncovered three serines (S75, S87, and S105) in the N-terminus of hER? as targets of ERK1/2 and p38 kinases. We raised a specific antibody against phosphorylated S105 (pS105) and demonstrated that this site was endogenously phosphorylated in MDA-MB-231 and BT-474 cells. A phospho-mimetic mutant generated from hER?1 was found to exhibit higher transactivation activity than hER?1. Ectopic expression of this mutant inhibited cell migration and invasion, but did not affect cell growth and cell-cycle progression in these cell models. In breast cancer specimens, pS105-hER? immunoreactivity was detected with a higher prevalence and intensity than that of hER?1. These results underscore the functional importance of the first experimentally identified hER?-phosphorylation site in breast cancer.

SUBMITTER: Lam HM 

PROVIDER: S-EPMC3348253 | biostudies-other | 2012 Jul

REPOSITORIES: biostudies-other

altmetric image

Publications

Phosphorylation of human estrogen receptor-beta at serine 105 inhibits breast cancer cell migration and invasion.

Lam Hung-Ming HM   Suresh Babu C V CV   Wang Jiang J   Yuan Yong Y   Lam Ying-Wai YW   Ho Shuk-Mei SM   Leung Yuet-Kin YK  

Molecular and cellular endocrinology 20120219 1


Multiple phosphorylation sites on the human estrogen receptor (hER)α were identified and shown to influence mammary carcinogenesis. In contrast, functional phosphorylation sites of hERβ have yet to be experimentally identified and validated. Here, using mass spectrometry, we uncovered three serines (S75, S87, and S105) in the N-terminus of hERβ as targets of ERK1/2 and p38 kinases. We raised a specific antibody against phosphorylated S105 (pS105) and demonstrated that this site was endogenously  ...[more]

Similar Datasets

| S-EPMC6694553 | biostudies-literature
| S-EPMC3873424 | biostudies-literature
| S-EPMC4033595 | biostudies-literature
| S-EPMC3423624 | biostudies-literature
| S-EPMC6257197 | biostudies-literature
| S-EPMC4518221 | biostudies-literature
| S-EPMC8570087 | biostudies-literature
2022-01-01 | GSE190238 | GEO
| S-EPMC9097292 | biostudies-literature
2024-07-31 | GSE266982 | GEO