Evidence map›Paper›PMID 17875942›Full record

ArticleMolecular and cellular biology2007

Regulation of neuron survival through an intersectin-phosphoinositide 3'-kinase C2beta-AKT pathway.

Margaret Das, Erica Scappini, Negin P Martin, Katy A Wong, Sara Dunn, Yun-Ju Chen, Stephanie L H Miller, Jan Domin, John P O'Bryan

Abstract read
In one paragraph

Article in Molecular and cellular biology, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers.

0numbers the graph read from it
0cells of the map it votes in
37citing papers in PubMed
2.4field-weighted citation impact, top 12% 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

37 citing papers in PubMed, 76 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. An Overview of Class II Phosphoinositide 3-Kinases.Current topics in microbiology and immunology · 2022
    Article
  5. Article
  6. Article
  7. Article
  8. Review
  9. Review
  10. Article
  11. Silencing Intersectin 1 Slows Orthotopic Neuroblastoma Growth in Mice.Journal of pediatric hematology/oncology · 2017
    Article
  12. Article
  13. Article
  14. Intersectin scaffold proteins and their role in cell signaling and endocytosis.Biochimica et biophysica acta. Molecular cell research · 2017
    Review
  15. Article
  16. Review
  17. Article
  18. Article
  19. Review
  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

9 authors at 7 institutions in 2 countries.

Margaret DasLaboratory of Signal Transduction, Laboratory of Neurobiology, National Institute of Environmental Health Sciences, National Institutes of Health, Department of Health and Human Services, Research Triangle Park, North Carolina 27709, USA.
Erica Scappini
Negin P Martin
Katy A Wong
Sara Dunn
Yun-Ju Chen
Stephanie L H Miller
Jan Domin
John P O'Bryan
University of Illinois Chicago · USIllinois College · USImperial College London · GBNational Institute of Environmental Health Sciences · USNational Institutes of Health · USUniversity of Illinois Urbana-Champaign · USUniversity of North Carolina at Chapel Hill · US

Funding

Intramural NIH HHSMedical Research Council G0500936
6 · The paper itself

Abstract

While endocytosis attenuates signals from plasma membrane receptors, recent studies suggest that endocytosis also serves as a platform for the compartmentalized activation of cellular signaling pathways. Intersectin (ITSN) is a multidomain scaffolding protein that regulates endocytosis and has the potential to regulate various biochemical pathways through its multiple, modular domains. To address the biological importance of ITSN in regulating cellular signaling pathways versus in endocytosis, we have stably silenced ITSN expression in neuronal cells by using short hairpin RNAs. Decreasing ITSN expression dramatically increased apoptosis in both neuroblastoma cells and primary cortical neurons. Surprisingly, the loss of ITSN did not lead to major defects in the endocytic pathway. Yeast two-hybrid analysis identified class II phosphoinositide 3'-kinase C2beta (PI3K-C2beta) as an ITSN binding protein, suggesting that ITSN may regulate a PI3K-C2beta-AKT survival pathway. ITSN associated with PI3K-C2beta on a subset of endomembrane vesicles and enhanced both basal and growth factor-stimulated PI3K-C2beta activity, resulting in AKT activation. The use of pharmacological inhibitors, dominant negatives, and rescue experiments revealed that PI3K-C2beta and AKT were epistatic to ITSN. This study represents the first demonstration that ITSN, independent of its role in endocytosis, regulates a critical cellular signaling pathway necessary for cell survival.

Indexed as

Cell SurvivalAdaptor Proteins, Vesicular TransportAmino Acid SequenceAnimalsCell LineEndocytosisEnzyme ActivationEpidermal Growth FactorEpistasis, GeneticHumansMiceMolecular Sequence DataNeuronsPhosphatidylinositol 3-KinasesPhosphoinositide-3 Kinase InhibitorsProtein IsoformsAdaptor Proteins, Vesicular TransportEpidermal Growth Factorintersectin 1Phosphatidylinositol 3-KinasesPhosphoinositide-3 Kinase InhibitorsProtein IsoformsProtein SubunitsProto-Oncogene Proteins c-aktRecombinant Fusion Proteins

Identifiers

PMID17875942
PMCPMC2169155
OpenAlexW2141061880

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.