Evidence map›Paper›PMID 25860340›Full record

ArticleMolecular endocrinology (Baltimore, Md.)2015

Clathrin Heavy Chain Interacts With Estrogen Receptor α and Modulates 17β-Estradiol Signaling.

Pierangela Totta, Valeria Pesiri, Masato Enari, Maria Marino, Filippo Acconcia

Abstract read
In one paragraph

Article in Molecular endocrinology (Baltimore, Md.), 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
2.7field-weighted citation impact, top 9% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

13 citing papers in PubMed, 28 citations in OpenAlex.

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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

5 authors at 2 institutions in 2 countries.

Pierangela TottaDepartment of Sciences (P.T., V.P., M.M., F.A.), Section Biomedical Sciences and Technology, University Roma Tre, I-00146, Rome, Italy; and Division of Refractory Cancer Research (M.E.), National Cancer Center Research Institute, Chuo-ku, Tokyo 104-0045, Japan.
Valeria Pesiri
Masato Enari
Maria Marino
Filippo Acconcia
Roma Tre University · ITNational Cancer Center · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

17β-estradiol (E2)-induced signaling and control of estrogen receptor (ER)α degradation both play a major role in breast cancer cell proliferation. We recently reported the involvement of lysosomal function in both E2-dependent ERα breakdown and E2-induced cell proliferation and thus hypothesized a role for endocytic proteins in ERα signaling. An small interfering RNA screen identified proteins that regulate intracellular endocytic traffic and whose silencing alters E2-induced ERα degradation. One such protein was the clathrin heavy chain (CHC), whose role in E2:ERα signaling to cell proliferation is unknown. Here, we show that CHC physically interacts with ERα in the cytoplasm of breast cancer cells and regulates E2-induced cell proliferation. Surprisingly, the CHC:ERα interaction is required to sustain E2 signaling but is dispensable for ERα degradation. Our data also demonstrate that many membrane trafficking proteins contribute to the regulation of ERα degradation, thus unraveling the contribution of endocytic proteins in E2:ERα signaling.

Indexed as

Cell ProliferationClathrin Heavy ChainsEndocytosisEstradiolEstrogen Receptor alphaHumansMCF-7 CellsPalmitic AcidProtein BindingProtein Interaction MappingProtein Processing, Post-TranslationalProteolysisReceptor, IGF Type 1Signal TransductionClathrin Heavy ChainsESR1 protein, humanEstradiolEstrogen Receptor alphaPalmitic AcidReceptor, IGF Type 1

Identifiers

PMID25860340
PMCPMC5414742
OpenAlexW2164750723

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.