Evidence map›Paper›PMID 22139091›Full record

ArticlePurinergic signalling2012

P2Y12 receptor expression is a critical determinant of functional responsiveness to ATX's MORFO domain.

Jameel Dennis, Magdalena K Morgan, Martin R Graf, Babette Fuss

Open access · bronzeAbstract read
In one paragraph

Article in Purinergic signalling, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
0.7field-weighted citation impact, top 29% 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

15 citing papers in PubMed, 20 citations in OpenAlex.

  1. Article
  2. Lysophosphatidic acid signaling via LPAJournal of neurochemistry · 2022
    Article
  3. Review
  4. Article
  5. Article
  6. Article
  7. Review
  8. Review
  9. Article
  10. Review
  11. The Autotaxin-Lysophosphatidic Acid Axis Modulates Histone Acetylation and Gene Expression during Oligodendrocyte Differentiation.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2015
    Article
  12. Article
  13. Revisiting the matricellular concept.Matrix biology : journal of the International Society for Matrix Biology · 2014
    Review
  14. Article
  15. 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

4 authors at 2 institutions in 1 country.

Jameel DennisDepartment of Anatomy, Virginia Commonwealth University Medical Center, Richmond, VA 23298, USA. jdennis@genciabiotech.com
Magdalena K Morgan
Martin R Graf
Babette Fuss
Virginia Commonwealth University Medical Center · USVirginia Commonwealth University · US

Funding

Virus Vector Shared ResourceP30CA016059 · NCI · VIRGINIA COMMONWEALTH UNIVERSITY · PI Kim Felder Rhoads · 1985 to 2026
$51.0M
VCU Neuroscience Center Core GrantP30NS047463 · NINDS · VIRGINIA COMMONWEALTH UNIVERSITY · PI POVLISHOCK, JOHN T · 2003 to 2013
$5.0M
Mechanisms in CNS myelination: Role of PD-lalpha/ATXR01NS045883 · NINDS · VIRGINIA COMMONWEALTH UNIVERSITY · PI FUSS, BABETTE · 2004 to 2020
$4.5M
NCI NIH HHS 5 P30 CA016059NCI NIH HHS P30 CA016059NINDS NIH HHS 5 P30 NS047463NINDS NIH HHS P30 NS047463
6 · The paper itself

Abstract

In the central nervous system, the formation of the myelin sheath and the differentiation of the myelinating cells, namely oligodendrocytes, are regulated by complex signaling networks that involve purinergic receptors and the extracellular matrix. However, the exact nature of the molecular interactions underlying these networks still needs to be defined. In this respect, the data presented here reveal a signaling mechanism that is characterized by an interaction between the purinergic P2Y(12) receptor and the matricellular extracellular matrix protein autotaxin (ATX), also known as ENPP2, phosphodiesterase-Iα/ATX, or lysoPLD. ATX has been previously described by us to mediate intermediate states of oligodendrocyte adhesion and to enable changes in oligodendrocyte morphology that are thought to be crucial for the formation of a fully functional myelin sheath. This functional property of ATX is mediated by ATX's modulator of oligodendrocyte remodeling and focal adhesion organization (MORFO) domain. Here, we show that the expression of the P2Y(12) receptor is necessary for ATX's MORFO domain to exert its effects on differentiating oligodendrocytes. In addition, our data demonstrate that exogenous expression of the P2Y(12) receptor can render cells responsive to the known effects of ATX's MORFO domain, and they identify Rac1 as an intracellular factor mediating the effect of ATX-MORFO-P2Y(12) signaling on the assembly of focal adhesions. Our data further support the idea that a physical interaction between ATX and the P2Y(12) receptor provides the basis for an ATX-MORFO-P2Y(12) signaling axis that is crucial for mediating cellular states of intermediate adhesion and morphological/structural plasticity.

Indexed as

Gene Expression RegulationAnimalsAnimals, NewbornCells, CulturedCHO CellsCricetinaeCricetulusFemaleFocal AdhesionsHumansLysophospholipase DOligodendrogliaPhosphoric Diester HydrolasesProtein Structure, TertiaryRatsRats, Sprague-DawleyLysophospholipase DP2ry12 protein, ratPhosphoric Diester HydrolasesReceptors, Purinergic P2Receptors, Purinergic P2Y12

Identifiers

PMID22139091
PMCPMC3350589
OpenAlexW2052932605

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.