Cited by 72Estrogen and related hormone effectsReceptor Mechanisms and SignalingGenomics and Chromatin Dynamics

Kinases and protein phosphorylation as regulators of steroid hormone action

Open access
Weigel, Nancy L., Moore, Nicole L.·2007·Nuclear Receptor Signaling

Abstract

Although the primary signal for the activation of steroid hormone receptors is binding of hormone, there is increasing evidence that the activities of cell signaling pathways and the phosphorylation status of these transcription factors and their coregulators determine the overall response to the hormone. In some cases, enhanced cell signaling is sufficient to cause activation of receptors in medium depleted of steroids. Steroid receptors are targets for multiple kinases. Many of the phosphorylation sites contain Ser/Thr-Pro motifs implicating proline-directed kinases such as the cyclin-dependent kinases and the mitogen-activated kinases (MAPK) in receptor phosphorylation. Although some sites are constitutively phosphorylated, others are phosphorylated in response to hormone. Still others are only phosphorylated in response to specific cell signaling pathways. Phosphorylation of specific sites has been implicated not only in overall transcriptional activity, but also in nuclear localization, protein stability, and DNA binding. The studies of the roles of phosphorylation in coregulator function are more limited, but it is now well established that many of them are highly phosphorylated and that phosphorylation regulates their function. There is good evidence that some of the phosphorylation sites in the receptors and coregulators are targets of multiple signaling pathways. Individual sites have been associated both with functions that enhance the activity of the receptor, as well as with functions that inhibit activity. Thus, the specific combinations of phosphorylations of the steroid receptor combined with the expression levels and phosphorylation status of coregulators will determine the genes regulated and the biological response.

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.

A few free checks a day · papers already verified open instantly · results are public

Integrity signals

Registry

Crossref · 10.1621/nrs.05005

Cites

124 of 124 references verified0 citation errors · 0 not checkable

Statistics

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.

A few free checks a day · papers already verified open instantly · results are public

Claims other papers make about this one

Each is checked against this paper’s own text: does it say what the citing paper says it does?

  • Animal steroid hormones exert their actions via binding to their intracellular nuclear receptors.

    “Animal steroid hormones are known exert their actions via binding to their intracellular nuclear receptors [7], for example, estrogen binds to its nuclear estrogen receptors ERα and ERβ [8], androgens bind to androgen receptors (AR) [9], and glucocorticoids bind to glucocorticoid receptors [10].”

Self-check

Percentages, sums and reported differences re-computed from the paper’s own numbers.

The self-check needs the paper’s full text.

Cites

1 retracted

Flagged first, then by citations

Cited by

Sorted by citations

Authors
Weigel, N. L., & Moore, N. L.
Affiliations
Baylor College of Medicine (US)
Corresponding author
Weigel, Nancy L.
Venue
Nuclear Receptor Signaling
Published
2007-01
Volume
5
Issue
1
Pages
e005-e005
ISSN
1550-7629 (ISSN-L)
OpenAlex
W1987431548
Cited by
72
References
124
Citations by year
2025: 2 · 2024: 5 · 2023: 2 · 2022: 1 · 2021: 2 · 2020: 1 · 2019: 2 · 2018: 4 · 2016: 3 · 2015: 2 · 2014: 2 · 2013: 13 · 2012: 2
FWCI
0.91
Type
journal article
Language
en
Open access
Locations
  • Nuclear Receptor Signaling (publishedVersion, cc-by-nc)
  • PubMed Central (publishedVersion, other-oa)
  • PubMed (publishedVersion)
  • Adelaide Research & Scholarship (AR&S) (University of Adelaide) (submittedVersion, other-oa)
Funders
National Cancer Institute (R01-CA57539, R01CA057539)
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Estrogen and related hormone effects
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Receptor Mechanisms and Signaling
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Genomics and Chromatin Dynamics
Keywords
steroid hormone receptors, protein phosphorylation, kinases, coregulators, cyclin-dependent kinases, mitogen-activated protein kinase, proline-directed phosphorylation, transcriptional regulation, nuclear localization, protein stability, DNA binding, signaling pathways
MeSH terms
Cell Nucleus, Feedback, Models, Biological, Nuclear Proteins, Phosphorylation, Phosphotransferases, Gonadal Steroid Hormones, Signal Transduction, Receptors, Cytoplasmic and Nuclear

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