Abstract
The identification and subsequent cloning of the 66-kDa human estrogen receptor (here termed hER-α66), its 46-kDa splice variant hER-α46, and the closely related hER-β have had a profound impact on the generation of new understanding of estrogen-mediated functions and led to progress in diagnosis and treatment of human breast cancer. However, a persistent problem has been that not all findings previously reported in estrogen-stimulated cell proliferation can be explained through the known properties of the different estrogen receptors described. As the consequence of a search for alternative mechanisms to account for these different findings, we have now identified, cloned, and expressed in HEK 293 cells a previously unrecognized 36-kDa variant of hER-α66, termed hER-α36. hER-α36 differs from hER-α66 since it lacks both transcriptional activation domains (AF-1 and AF-2) but it retains the DNA-binding domain, and partial dimerization and ligand-binding domains of hER-α66. It also contains three myristoylation sites postulated to direct ER-α36 to the plasma membrane. It is concluded that ER-α36 is a unique variant of ER-α66; ER-α36 is predicted to function as a dominant-negative effector of hER-α66-mediated estrogen-responsive gene pathways and has the potential to trigger membrane-initiated mitogenic estrogen signaling.
| Original language | English |
|---|---|
| Pages (from-to) | 1023-1027 |
| Number of pages | 5 |
| Journal | Biochemical and Biophysical Research Communications |
| Volume | 336 |
| Issue number | 4 |
| DOIs | |
| State | Published - Nov 4 2005 |
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All Science Journal Classification (ASJC) codes
- Biochemistry
- Biophysics
- Molecular Biology
Cite this
Identification, cloning, and expression of human estrogen receptor-α36, a novel variant of human estrogen receptor-α66. / Zhao, Yi Wang; Zhang, XinTian; Shen, Peng; Loggie, Brian W.; Chang, YunChao; Deuel, Thomas F.
In: Biochemical and Biophysical Research Communications, Vol. 336, No. 4, 04.11.2005, p. 1023-1027.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Identification, cloning, and expression of human estrogen receptor-α36, a novel variant of human estrogen receptor-α66
AU - Zhao, Yi Wang
AU - Zhang, XinTian
AU - Shen, Peng
AU - Loggie, Brian W.
AU - Chang, YunChao
AU - Deuel, Thomas F.
PY - 2005/11/4
Y1 - 2005/11/4
N2 - The identification and subsequent cloning of the 66-kDa human estrogen receptor (here termed hER-α66), its 46-kDa splice variant hER-α46, and the closely related hER-β have had a profound impact on the generation of new understanding of estrogen-mediated functions and led to progress in diagnosis and treatment of human breast cancer. However, a persistent problem has been that not all findings previously reported in estrogen-stimulated cell proliferation can be explained through the known properties of the different estrogen receptors described. As the consequence of a search for alternative mechanisms to account for these different findings, we have now identified, cloned, and expressed in HEK 293 cells a previously unrecognized 36-kDa variant of hER-α66, termed hER-α36. hER-α36 differs from hER-α66 since it lacks both transcriptional activation domains (AF-1 and AF-2) but it retains the DNA-binding domain, and partial dimerization and ligand-binding domains of hER-α66. It also contains three myristoylation sites postulated to direct ER-α36 to the plasma membrane. It is concluded that ER-α36 is a unique variant of ER-α66; ER-α36 is predicted to function as a dominant-negative effector of hER-α66-mediated estrogen-responsive gene pathways and has the potential to trigger membrane-initiated mitogenic estrogen signaling.
AB - The identification and subsequent cloning of the 66-kDa human estrogen receptor (here termed hER-α66), its 46-kDa splice variant hER-α46, and the closely related hER-β have had a profound impact on the generation of new understanding of estrogen-mediated functions and led to progress in diagnosis and treatment of human breast cancer. However, a persistent problem has been that not all findings previously reported in estrogen-stimulated cell proliferation can be explained through the known properties of the different estrogen receptors described. As the consequence of a search for alternative mechanisms to account for these different findings, we have now identified, cloned, and expressed in HEK 293 cells a previously unrecognized 36-kDa variant of hER-α66, termed hER-α36. hER-α36 differs from hER-α66 since it lacks both transcriptional activation domains (AF-1 and AF-2) but it retains the DNA-binding domain, and partial dimerization and ligand-binding domains of hER-α66. It also contains three myristoylation sites postulated to direct ER-α36 to the plasma membrane. It is concluded that ER-α36 is a unique variant of ER-α66; ER-α36 is predicted to function as a dominant-negative effector of hER-α66-mediated estrogen-responsive gene pathways and has the potential to trigger membrane-initiated mitogenic estrogen signaling.
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U2 - 10.1016/j.bbrc.2005.08.226
DO - 10.1016/j.bbrc.2005.08.226
M3 - Article
VL - 336
SP - 1023
EP - 1027
JO - Biochemical and Biophysical Research Communications
JF - Biochemical and Biophysical Research Communications
SN - 0006-291X
IS - 4
ER -