Evidence map›Paper›PMID 15772345›Full record

ArticleThe Journal of neuroscience : the official journal of the Society for Neuroscience2005

Signaling microdomains regulate inositol 1,4,5-trisphosphate-mediated intracellular calcium transients in cultured neurons.

Simon N Jacob, Chi-Un Choe, Per Uhlen, Brenda DeGray, Mark F Yeckel, Barbara E Ehrlich

Abstract readComparative Study
In one paragraph

Article in The Journal of neuroscience : the official journal of the Society for Neuroscience, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
–field-weighted citation impact
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

21 citing papers in PubMed.

  1. Article
  2. Article
  3. Comparison of CaCell calcium · 2017
    Article
  4. Article
  5. Article
  6. Article
  7. Review
  8. Review
  9. Article
  10. Article
  11. Article
  12. Article
  13. Review
  14. Inositol trisphosphate 3-kinases: focus on immune and neuronal signaling.Cellular and molecular life sciences : CMLS · 2010
    Review
  15. Secretory granules in inositol 1,4,5-trisphosphate-dependent Ca2+ signaling in the cytoplasm of neuroendocrine cells.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2010
    Review
  16. Article
  17. Article
  18. Article
  19. 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

6 authors.

Simon N JacobDepartment of Pharmacology, Yale University, New Haven, Connecticut 06520, USA.
Chi-Un Choe
Per Uhlen
Brenda DeGray
Mark F Yeckel
Barbara E Ehrlich

Funding

Regulation of cholangiocytes by InsP3 receptor isoformsR01DK061747 · NIDDK · YALE UNIVERSITY · PI EHRLICH, BARBARA E., NATHANSON, MICHAEL H · 2003 to 2012
$3.4M
The Function of Ca2+ Waves In Hippocampal Neurons.R01MH067830 · NIMH · YALE UNIVERSITY · PI YECKEL, MARK F · 2004 to 2008
$1.5M
Dynamic Interactions of IP3 Receptor LigandsR01GM063496 · NIGMS · YALE UNIVERSITY · PI EHRLICH, BARBARA E. · 2001 to 2004
$1.1M
NIDDK NIH HHS DK61747NIDDK NIH HHS R01 DK061747NIGMS NIH HHS GM63496NIGMS NIH HHS R01 GM063496NIMH NIH HHS MH67830NIMH NIH HHS R01 MH067830
6 · The paper itself

Abstract

Ca2+ signals in neurons use specific temporal and spatial patterns to encode unambiguous information about crucial cellular functions. To understand the molecular basis for initiation and propagation of inositol 1,4,5-trisphosphate (InsP3)-mediated intracellular Ca2+ signals, we correlated the subcellular distribution of components of the InsP3 pathway with measurements of agonist-induced intracellular Ca2+ transients in cultured rat hippocampal neurons and pheochromocytoma cells. We found specialized domains with high levels of phosphatidylinositol-4-phosphate kinase (PIPKI) and chromogranin B (CGB), proteins acting synergistically to increase InsP3 receptor (InsP3R) activity and sensitivity. In contrast, Ca2+ pumps in the plasma membrane (PMCA) and sarco-endoplasmic reticulum as well as buffers that antagonize the rise in intracellular Ca2+ were distributed uniformly. By pharmacologically blocking phosphatidylinositol-4-kinase and PIPKI or disrupting the CGB-InsP3R interaction by transfecting an interfering polypeptide fragment, we produced major changes in the initiation site and kinetics of the Ca2+ signal. This study shows that a limited number of proteins can reassemble to form unique, spatially restricted signaling domains to generate distinctive signals in different regions of the same neuron. The finding that the subcellular location of initiation sites and protein microdomains was cell type specific will help to establish differences in spatiotemporal Ca2+ signaling in different types of neurons.

Indexed as

AnimalsCalciumCalcium ChannelsCalcium SignalingCalcium-Transporting ATPasesCarbacholCation Transport ProteinsCells, CulturedCholinergic AgonistsDose-Response Relationship, DrugDrug InteractionsEmbryo, MammalianEndoplasmic ReticulumEnzyme InhibitorsHippocampusImmunohistochemistry3,4-dihydroxyphenylglycolCalciumCalcium ChannelsCalcium-Transporting ATPasesCarbacholCation Transport ProteinsCholinergic AgonistsEnzyme InhibitorsInositol 1,4,5-Trisphosphate Receptorsmetabotropic glutamate receptor type 1MethoxyhydroxyphenylglycolNerve Growth FactorParvalbuminsPeptide FragmentsPlasma Membrane Calcium-Transporting ATPasesReceptors, Cytoplasmic and NuclearReceptors, Metabotropic GlutamateSarcoplasmic Reticulum Calcium-Transporting ATPases

Identifiers

PMID15772345
PMCPMC2951020

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.