Evidence map›Paper›PMID 20544340›Full record

ReviewCurrent topics in microbiology and immunology2010

The regulation of class IA PI 3-kinases by inter-subunit interactions.

Jonathan M Backer

Abstract readReview
In one paragraph

Review in Current topics in microbiology and immunology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 56 papers.

0numbers the graph read from it
0cells of the map it votes in
56citing papers in PubMed
5.8field-weighted citation impact, top 4% 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

56 citing papers in PubMed, 94 citations in OpenAlex.

  1. Article
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  3. Review
  4. Article
  5. Article
  6. The role of SUMOylation in epithelial-mesenchymal transition.Journal of molecular medicine (Berlin, Germany) · 2025
    Review
  7. Influenza A virus NS1 protein mimics oncogenic PI3K resulting in isoform specific cellular redistribution and activation.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  8. Functional selection in SH3-mediated activation of the PI3 kinase.bioRxiv : the preprint server for biology · 2024
    Article
  9. Review
  10. Article
  11. Review
  12. Review
  13. Article
  14. Article
  15. Article
  16. Article
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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

1 author at 1 institution in 1 country.

Jonathan M BackerDepartment of Molecular Pharmacology, Albert Einstein College of Medicine, Bronx, NY, 10461, USA. jonathan.backer@einstein.yu.edu
Albert Einstein College of Medicine · US

Funding

Tumor Progression and MetastasisP01CA100324 · NCI · YESHIVA UNIVERSITY · PI CONDEELIS, JOHN S · 2003 to 2018
$30.0M
P85/P110 PI 3 KINASE--STRUCTURE/FUNCTION AND PHYSIOLOGYR01GM055692 · NIGMS · YESHIVA UNIVERSITY · PI BACKER, JONATHAN M. · 1997 to 2013
$4.4M
NCI NIH HHS 1P01 CA100324NCI NIH HHS P01 CA100324NIDDK NIH HHS DK07069NIGMS NIH HHS GM55692NIGMS NIH HHS R01 GM055692
6 · The paper itself

Abstract

Phosphoinositide 3-kinases (PI 3-kinases) are activated by growth factor and hormone receptors, and regulate cell growth, survival, motility, and responses to changes in nutritional conditions (Engelman et al. 2006). PI 3-kinases have been classified according to their subunit composition and their substrate specificity for phosphoinositides (Vanhaesebroeck et al. 2001). The class IA PI 3-kinase is a heterodimer consisting of one regulatory subunit (p85α, p85β, p55α, p50α, or p55γ) and one 110-kDa catalytic subunit (p110α, β or δ). The Class IB PI 3-kinase is also a dimer, composed of one regulatory subunit (p101 or p87) and one catalytic subunit (p110γ) (Wymann et al. 2003). Class I enzymes will utilize PI, PI[4]P, or PI[4,5]P2 as substrates in vitro, but are thought to primarily produce PI[3,4,5]P3 in cells.The crystal structure of the Class IB PI 3-kinase catalytic subunit p110γ was solved in 1999 (Walker et al. 1999), and crystal or NMR structures of the Class IA p110α catalytic subunit and all of the individual domains of the Class IA p85α regulatory subunit have been solved (Booker et al. 1992; Günther et al. 1996; Hoedemaeker et al. 1999; Huang et al. 2007; Koyama et al. 1993; Miled et al. 2007; Musacchio et al. 1996; Nolte et al. 1996; Siegal et al. 1998). However, a structure of an intact PI 3-kinase enzyme has remained elusive. In spite of this, studies over the past 10 years have lead to important insights into how the enzyme is regulated under physiological conditions. This chapter will specifically discuss the regulation of Class IA PI 3-kinase enzymatic activity, focusing on regulatory interactions between the p85 and p110 subunits and the modulation of these interactions by physiological activators and oncogenic mutations. The complex web of signaling downstream from Class IA PI 3-kinases will be discussed in other chapters in this volume.

Indexed as

AnimalsEnzyme ActivationHumansMutationPhosphatidylinositol 3-KinasesPhosphorylationProtein Structure, TertiaryProtein Subunitssrc Homology DomainsPhosphatidylinositol 3-KinasesProtein Subunits

Identifiers

PMID20544340
PMCPMC3234103
OpenAlexW3169518

What Socratic holds

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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.