Ontology highlight
ABSTRACT:
SUBMITTER: Lam HM
PROVIDER: S-EPMC3348253 | biostudies-other | 2012 Jul
REPOSITORIES: biostudies-other
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]