Evidence map›Paper›PMID 10921882›Full record

ArticleThe EMBO journal2000

Negative regulation of PI 3-kinase by Ruk, a novel adaptor protein.

I Gout, G Middleton, J Adu, N N Ninkina, L B Drobot, V Filonenko, G Matsuka, A M Davies, M Waterfield, V L Buchman

Open access · bronzeAbstract read
In one paragraph

Article in The EMBO journal, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 49 papers.

0numbers the graph read from it
0cells of the map it votes in
49citing papers in PubMed
3.7field-weighted citation impact, top 6% 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

49 citing papers in PubMed, 139 citations in OpenAlex.

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  10. Amyloid precursor protein and endosomal-lysosomal dysfunction in Alzheimer's disease: inseparable partners in a multifactorial disease.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2017
    Review
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  14. Capping protein regulators fine-tune actin assembly dynamics.Nature reviews. Molecular cell biology · 2014
    Review
  15. Article
  16. Article
  17. CD2AP regulates SUMOylation of CIN85 in podocytes.Molecular and cellular biology · 2012
    Article
  18. Article
  19. CIN85 interacting proteins in B cells-specific role for SHIP-1.Molecular & cellular proteomics : MCP · 2011
    Article
  20. Article
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

10 authors at 4 institutions in 3 countries.

I GoutLudwig Institute for Cancer Research, Courtauld Building, 91 Riding House Street, London W1P 8BT, UK.
G Middleton
J Adu
N N Ninkina
L B Drobot
V Filonenko
G Matsuka
A M Davies
M Waterfield
V L Buchman
University of St Andrews · GBInstitute of Gene Biology · RULudwig Cancer Research · GBPalladin Institute of Biochemistry · UA

Funding

Viral Vector Technology (VVTSR)P30CA021765 · NCI · ST. JUDE CHILDREN'S RESEARCH HOSPITAL · PI CHARLES ROBERTS · 1985 to 2026
$166.9M
NCI NIH HHS CA21765Wellcome Trust
6 · The paper itself

Abstract

Class I(A) phosphatidylinositol 3-kinase (PI 3-kinase) is a key component of important intracellular signalling cascades. We have identified an adaptor protein, Ruk(l), which forms complexes with the PI 3-kinase holoenzyme in vitro and in vivo. This interaction involves the proline-rich region of Ruk and the SH3 domain of the p85 alpha regulatory subunit of the class I(A) PI 3-kinase. In contrast to many other adaptor proteins that activate PI 3-kinase, interaction with Ruk(l) substantially inhibits the lipid kinase activity of the enzyme. Overexpression of Ruk(l) in cultured primary neurons induces apoptosis, an effect that could be reversed by co-expression of constitutively activated forms of the p110 alpha catalytic subunit of PI 3-kinase or its downstream effector PKB/Akt. Our data provide evidence for the existence of a negative regulator of the PI 3-kinase signalling pathway that is essential for maintaining cellular homeostasis. Structural similarities between Ruk, CIN85 and CD2AP/CMS suggest that these proteins form a novel family of adaptor molecules that are involved in various intracellular signalling pathways.

Indexed as

Neoplasm ProteinsPhosphoinositide-3 Kinase InhibitorsAdaptor Proteins, Signal TransducingAmino Acid SequenceAnimalsApoptosisBinding SitesCloning, MolecularDNA, ComplementaryGene Expression Regulation, EnzymologicHumansMiceMolecular Sequence DataNerve Tissue ProteinsNeurons, AfferentPhosphatidylinositol 3-KinasesAdaptor Proteins, Signal TransducingDNA, ComplementaryNeoplasm ProteinsNerve Tissue ProteinsPhosphatidylinositol 3-KinasesPhosphoinositide-3 Kinase InhibitorsProtein IsoformsRecombinant ProteinsSh3kbp1 protein, mouse

Identifiers

PMID10921882
PMCPMC306608
OpenAlexW2170770662

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.