The DOI matches its Crossref record; 44 of the 44 references it cites were found in a registry or an index.
Palmitoylation-dependent Estrogen Receptor α Membrane Localization: Regulation by 17β-Estradiol
Open accessAbstract
A fraction of the nuclear estrogen receptor α (ERα) is localized to the plasma membrane region of 17β-estradiol (E2) target cells. We previously reported that ERα is a palmitoylated protein. To gain insight into the molecular mechanism of ERα residence at the plasma membrane, we tested both the role of palmitoylation and the impact of E2 stimulation on ERα membrane localization. The cancer cell lines expressing transfected or endogenous human ERα (HeLa and HepG2, respectively) or the ERα nonpalmitoylable Cys447Ala mutant transfected in HeLa cells were used as experimental models. We found that palmitoylation of ERα enacts ERα association with the plasma membrane, interaction with the membrane protein caveolin-1, and nongenomic activities, including activation of signaling pathways and cell proliferation (i.e., ERK and AKT activation, cyclin D 1 promoter activity, DNA synthesis). Moreover, E2 reduces both ERα palmitoylation and its interaction with caveolin-1, in a time- and dose-dependent manner. These data point to the physiological role of ERα palmitoylation in the receptor localization to the cell membrane and in the regulation of the E2-induced cell proliferation.
Overview
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
Cites
Bradford, M. M. (1976) · Analytical Biochemistry · doi:10.1016/0003-2697(76)90527-3 · Cited by 255,302
Molecular basis of agonism and antagonism in the oestrogen receptor
Brzozowski, A. M., Pike, A. C. W., Dauter, Z., Hubbard, R. E., Bonn, T., Engström, O., Öhman, L., Greene, G. L., Gustafsson, J.-Å., & Carlquist, M. (1997) · Nature · doi:10.1038/39645 · Cited by 3,355
Interaction of oestrogen receptor with the regulatory subunit of phosphatidylinositol-3-OH kinase
Simoncini, T., Hafezi-Moghadam, A., Brazil, D. P., Ley, K., Chin, W. W., & Liao, J. K. (2000) · Nature · doi:10.1038/35035131 · Cited by 1,436
Resh, M. D. (1999) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/s0167-4889(99)00075-0 · Cited by 1,250
Nongenotropic, Sex-Nonspecific Signaling through the Estrogen or Androgen Receptors
Kousteni, S., Bellido, T., Plotkin, L. I., O'Brien, C. A., Bodenner, D. L., Han, L., Han, K., DiGregorio, G. B., Katzenellenbogen, J. A., Katzenellenbogen, B. S., et al. (2001) · Cell · doi:10.1016/s0092-8674(01)00268-9 · Cited by 1,113
Razandi, M., Pedram, A., Greene, G. L., & Levin, E. R. (1999) · Molecular Endocrinology · doi:10.1210/mend.13.2.0239 · Cited by 1,040
Kousteni, S. (2001) · Cell · doi:10.1016/s0092-8674(02)08100-x · Cited by 746
Reid, G., Hübner, M. R., Métivier, R., Brand, H., Denger, S., Manu, D., Beaudouin, J., Ellenberg, J., & Gannon, F. (2003) · Molecular Cell · doi:10.1016/s1097-2765(03)00090-x · Cited by 732
Rapid actions of plasma membrane estrogen receptors
Kelly, M. J., & Levin, E. R. (2001) · Trends in Endocrinology & Metabolism · doi:10.1016/s1043-2760(01)00377-0 · Cited by 643
Toran-Allerand, C. D., Guan, X., MacLusky, N. J., Horvath, T. L., Diano, S., Singh, M., Connolly, E. S., Nethrapalli, I. S., & Tinnikov, A. A. (2002) · The Journal of Neuroscience · doi:10.1523/jneurosci.22-19-08391.2002 · Cited by 548
Cited by
Integration of the extranuclear and nuclear actions of estrogen
Levin, E. R. (2005) · Molecular Endocrinology · doi:10.1210/me.2004-0390 · Cited by 708
Extranuclear Steroid Receptors: Nature and Actions
Hammes, S. R., & Levin, E. R. (2007) · Endocrine Reviews · doi:10.1210/er.2007-0022 · Cited by 475
Estrogens, Neuroinflammation, and Neurodegeneration
Villa, A., Vegeto, E., Poletti, A., & Maggi, A. (2016) · Endocrine Reviews · doi:10.1210/er.2016-1007 · Cited by 423
Rapid non-genomic effects of corticosteroids and their role in the central stress response
Groeneweg, F. L., Karst, H., de Kloet, E. R., & Joëls, M. (2011) · Journal of Endocrinology · doi:10.1530/joe-10-0472 · Cited by 414
Palmitoylation of Ligands, Receptors, and Intracellular Signaling Molecules
Resh, M. D. (2006) · Science's STKE · doi:10.1126/stke.3592006re14 · Cited by 414
Metadata
- Authors
- Acconcia, F., Ascenzi, P., Bocedi, A., Spisni, E., Tomasi, V., Trentalance, A., Visca, P., & Marino, M.
- Venue
- Molecular Biology of the Cell
- Published
- 2005-01
- Volume
- 16
- Issue
- 1
- Pages
- 231-237
- ISSN
- 1059-1524 (ISSN-L)
- 1939-4586
- OpenAlex
- W2105846317
- Cited by
- 438
- References
- 44
- FWCI
- 9.93
- Type
- journal article
- Language
- en
- Open access
- green
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review
How to cite
Cite CoChat for the checks on this page, and the paper for its own findings.
- This page
- CoChat. (2026). Citation check: Palmitoylation-dependent Estrogen Receptor α Membrane Localization: Regulation by 17β-Estradiol. https://app.cochat.ai/papers/10.1091/mbc.e04-07-0547
- The paper
- Acconcia, F., Ascenzi, P., Bocedi, A., Spisni, E., Tomasi, V., Trentalance, A., Visca, P., & Marino, M. (2005). Palmitoylation-dependent Estrogen Receptor α Membrane Localization: Regulation by 17β-Estradiol. Molecular Biology of the Cell. https://doi.org/10.1091/mbc.e04-07-0547
Data sources
Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.
