Evidence map›Paper›PMID 22759789›Full record

ArticleCellular signalling2012

Identification of Ser/Thr phosphorylation sites in the C2-domain of phospholipase C γ2 (PLCγ2) using TRPM7-kinase.

Francina Deason-Towne, Anne-Laure Perraud, Carsten Schmitz

Open access · greenAbstract read
In one paragraph

Article in Cellular signalling, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 53 papers.

0numbers the graph read from it
0cells of the map it votes in
53citing papers in PubMed
5.2field-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

53 citing papers in PubMed, 81 citations in OpenAlex.

  1. Review
  2. Review
  3. Article
  4. Review
  5. MgScience advances · 2025
    Article
  6. TRPM channels in health and disease.Nature reviews. Nephrology · 2024
    Review
  7. Review
  8. Review
  9. Review
  10. Article
  11. Review
  12. Review
  13. Review
  14. Review
  15. Review
  16. Article
  17. Review
  18. Article
  19. Review
  20. Mapping TRPM7 Function by NS8593.International journal of molecular sciences · 2020
    Review
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

3 authors at 2 institutions in 1 country.

Francina Deason-TowneDepartment of Immunology, University of Colorado Denver, National Jewish Health, Denver, CO 80206, USA.
Anne-Laure Perraud
Carsten Schmitz
University of Colorado Denver · USNational Jewish Health · US

Funding

TRAINING PROGRAM IN IMMUNOLOGYT32AI007405 · NIAID · UNIVERSITY OF COLORADO DENVER · PI Laurel L Lenz, Raul Martin Torres · 1991 to 2026
$10.5M
Structure-function relationships of the chimeric TRPM7 channel-kinaseR01GM090123 · NIGMS · UNIVERSITY OF COLORADO DENVER · PI SCHMITZ, CARSTEN · 2010 to 2014
$1.4M
Cellular regulation of magnesium homeostasisR01GM068801 · NIGMS · NATIONAL JEWISH HEALTH · PI PERRAUD, ANNE-LAURE · 2004 to 2008
$1.3M
Modulation of PLCgamma2-Mediated Signaling Via its C2-Domain in B LymphocytesR21AI088421 · NIAID · UNIVERSITY OF COLORADO DENVER · PI SCHMITZ, CARSTEN · 2010 to 2011
$419k
The Role of Magnesium in B-Cell SignalingK08AI060926 · NIAID · UNIVERSITY OF COLORADO DENVER · PI SCHMITZ, CARSTEN · 2004 to 2006
$323k
NIAID NIH HHS K08 AI060926NIAID NIH HHS K08AI060926NIAID NIH HHS R21AI0088421NIAID NIH HHS R21 AI088421NIAID NIH HHS T32 AI007405NIAID NIH HHS T32 AI07405NIGMS NIH HHS R01 GM068801NIGMS NIH HHS R01GM068801NIGMS NIH HHS R01 GM090123NIGMS NIH HHS R01GM90123
6 · The paper itself

Abstract

PLC-isozymes are central elements of cellular signaling downstream of numerous receptors. PLCγ2 is a pivotal component of B cell receptor (BCR) signaling. The regulation of PLCγ2-dependent signaling functions by Tyr-phosphorylation is well characterized, however, the potential role of Ser/Thr phosphorylation events remains undefined. TRPM7 is the fusion of a Ser/Thr kinase with an ion channel, and an essential component of Mg(2+)-homeostasis regulation. Although the interaction between the C2 domain of several PLC-isozymes and TRPM7 is well established, previous studies have focused on the effect of PLC-activity on TRPM7. Here, we investigated whether Ser/Thr phosphorylation sites in the C2 domain of PLCγ2 could be identified using TRPM7-kinase. We show that TRPM7-kinase phosphorylates PLCγ2 in its C2-domain at position Ser1164 and in the linker region preceding the C2-domain at position Thr1045. Using a complementation approach in PLCγ2(-/-) DT40 cells, we found that the PLCγ2-S1164A mutant fully restores BCR mediated Ca(2+)-responses under standard growth conditions. However, under hypomagnesic conditions, PLCγ2-S1164A fails to reach Ca(2+)-levels seen in cells expressing PLCγ2 wildtype. These results suggest that Mg(2+)-sensitivity of the BCR signaling pathway may be regulated by Ser/Thr phosphorylation of PLCγ2.

Indexed as

Amino Acid SequenceAnimalsCalciumCell LineChickensHumansMagnesiumMolecular Sequence DataPhospholipase C gammaPhosphorylationProtein Serine-Threonine KinasesReceptors, Antigen, B-CellSerineSignal TransductionThreonineTRPM Cation ChannelsCalciumMagnesiumPhospholipase C gammaProtein Serine-Threonine KinasesReceptors, Antigen, B-CellSerineThreonineTRPM7 protein, humanTRPM Cation Channels

Identifiers

PMID22759789
PMCPMC4049354
OpenAlexW2087739235

What OpenQuestion holds

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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.