Evidence map›Paper›PMID 23622247›Full record

ArticleCell2013

14-3-3 proteins interact with a hybrid prenyl-phosphorylation motif to inhibit G proteins.

Philippe Riou, Svend Kjær, Ritu Garg, Andrew Purkiss, Roger George, Robert J Cain, Ganka Bineva, Nicolas Reymond, Brad McColl, Andrew J Thompson and 4 more

Erratum issuedOpen access · hybridAbstract read
In one paragraph

Article in Cell, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 68 papers.

0numbers the graph read from it
0cells of the map it votes in
68citing papers in PubMed
7.6field-weighted citation impact, top 2% 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

68 citing papers in PubMed, 104 citations in OpenAlex.

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  17. The RND1 Small GTPase: Main Functions and Emerging Role in Oncogenesis.International journal of molecular sciences · 2019
    Review
  18. Review
  19. Review
  20. Activated Rho GTPases in Cancer-The Beginning of a New Paradigm.International journal of molecular sciences · 2018
    Review

8 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

14 authors at 3 institutions in 1 country.

Philippe RiouRandall Division of Cell and Molecular Biophysics, New Hunt's House, King's College London, London, UK.
Svend Kjær
Ritu Garg
Andrew Purkiss
Roger George
Robert J Cain
Ganka Bineva
Nicolas Reymond
Brad McColl
Andrew J Thompson
Nicola O'Reilly
Neil Q McDonald
Peter J Parker
Anne J Ridley
King's College London · GBThe Honourable Society of Lincoln's Inn · GBCancer Research UK · GB

Funding

Biotechnology and Biological Sciences Research Council BB/E004083/1Biotechnology and Biological Sciences Research Council BB/E004083/2Cancer Research UK 10747Cancer Research UK 15683Cancer Research UK 15961Medical Research CouncilWellcome Trust
6 · The paper itself

Abstract

Signaling through G proteins normally involves conformational switching between GTP- and GDP-bound states. Several Rho GTPases are also regulated by RhoGDI binding and sequestering in the cytosol. Rnd proteins are atypical constitutively GTP-bound Rho proteins, whose regulation remains elusive. Here, we report a high-affinity 14-3-3-binding site at the C terminus of Rnd3 consisting of both the Cys241-farnesyl moiety and a Rho-associated coiled coil containing protein kinase (ROCK)-dependent Ser240 phosphorylation site. 14-3-3 binding to Rnd3 also involves phosphorylation of Ser218 by ROCK and/or Ser210 by protein kinase C (PKC). The crystal structure of a phosphorylated, farnesylated Rnd3 peptide with 14-3-3 reveals a hydrophobic groove in 14-3-3 proteins accommodating the farnesyl moiety. Functionally, 14-3-3 inhibits Rnd3-induced cell rounding by translocating it from the plasma membrane to the cytosol. Rnd1, Rnd2, and geranylgeranylated Rap1A interact similarly with 14-3-3. In contrast to the canonical GTP/GDP switch that regulates most Ras superfamily members, our results reveal an unprecedented mechanism for G protein inhibition by 14-3-3 proteins.

Indexed as

14-3-3 ProteinsAmino Acid SequenceAnimalsCell MembraneChlorocebus aethiopsCOS CellsCrystallography, X-RayCytosolHumansModels, MolecularMolecular Sequence DataPhosphorylationPrenylationProtein Interaction Domains and Motifsrho GTP-Binding Proteins14-3-3 Proteinsrho GTP-Binding ProteinsRND3 protein, humanYWHAZ protein, human

Identifiers

PMID23622247
PMCPMC3690454
OpenAlexW2124332747

What Socratic holds

Textmetadata
LicenceCC BY
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 Socratic graph.