Evidence map›Paper›PMID 16055744›Full record

ArticleMolecular and cellular biology2005

Binding of calmodulin to the carboxy-terminal region of p21 induces nuclear accumulation via inhibition of protein kinase C-mediated phosphorylation of Ser153.

Aina Rodríguez-Vilarrupla, Montserrat Jaumot, Neus Abella, Núria Canela, Sonia Brun, Carmen Díaz, Josep M Estanyol, Oriol Bachs, Neus Agell

Open access · greenAbstract read
In one paragraph

Article in Molecular and cellular biology, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
1.9field-weighted citation impact, top 14% 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

22 citing papers in PubMed, 43 citations in OpenAlex.

  1. Review
  2. Review
  3. The Emerging Role of p21 in Diabetes and Related Metabolic Disorders.International journal of molecular sciences · 2024
    Review
  4. CDKN1A/p21 in Breast Cancer: Part of the Problem, or Part of the Solution?International journal of molecular sciences · 2023
    Review
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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

9 authors at 1 institution in 1 country.

Aina Rodríguez-VilarruplaDepartment de Biologia Cel . lular, Fac. Medicina, Barcelona, Spain.
Montserrat Jaumot
Neus Abella
Núria Canela
Sonia Brun
Carmen Díaz
Josep M Estanyol
Oriol Bachs
Neus Agell
Universitat de Barcelona · ES

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Intracellular localization plays an important role in the functional regulation of the cell cycle inhibitor p21. We have previously shown that calmodulin binds to p21 and that calmodulin is essential for the nuclear accumulation of p21. Here, we analyze the mechanism of this regulation. We show that calmodulin inhibits in vitro phosphorylation of p21 by protein kinase C (PKC) and that this inhibition is dependent upon calmodulin binding to p21. Two-dimensional electrophoresis analysis of cells expressing the p21 wild type or p21S153A, a nonphosphorylatable mutant of p21 at position 153, indicates that Ser153 of p21 is a phosphorylable residue in vivo. Furthermore, Western blot analysis using phospho-Ser153-specific antibodies indicates that Ser153 phosphorylation in vivo is induced when PKC is activated and calmodulin is inhibited. The mutation of Ser153 to aspartate, a pseudophosphorylated residue, inhibits the nuclear accumulation of p21. Finally, whereas wild-type p21 translocates to the cytoplasm after PKC activation in the presence of calmodulin inhibitors, p21 carrying a nonphosphorylatable residue at position 153 remains in the nucleus. We propose that calmodulin binding to p21 prevents its phosphorylation by PKC at Ser153 and consequently allows its nuclear localization. When phosphorylated at Ser153, p21 is located at the cytoplasm and disrupts stress fibers.

Indexed as

Active Transport, Cell NucleusAnimalsBlotting, WesternCalmodulinCell Cycle ProteinsCell NucleusCOS CellsCyclin-Dependent Kinase Inhibitor p21CytoplasmElectrophoresis, Gel, Two-DimensionalGlutathione TransferaseGreen Fluorescent ProteinsImmunohistochemistryMiceMicroscopy, FluorescenceMutagenesis, Site-DirectedCalmodulinCdkn1a protein, mouseCell Cycle ProteinsCyclin-Dependent Kinase Inhibitor p21Glutathione TransferaseGreen Fluorescent ProteinsProliferating Cell Nuclear AntigenProtein Kinase CSerine

Identifiers

PMID16055744
PMCPMC1190259
OpenAlexW2121045332

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.