Evidence map›Paper›PMID 9265648›Full record

ArticleThe Journal of cell biology1997

Gelsolin modulates phospholipase C activity in vivo through phospholipid binding.

H q Sun, K m Lin, H L Yin

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of cell biology, 1997. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed
3.9field-weighted citation impact, top 5% 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

24 citing papers in PubMed, 93 citations in OpenAlex.

  1. Review
  2. Regulation of Mitochondrial Function by the Actin Cytoskeleton.Frontiers in cell and developmental biology · 2021
    Review
  3. Article
  4. Article
  5. Article
  6. Role and regulation of sperm gelsolin prior to fertilization.The Journal of biological chemistry · 2010
    Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Duplicated gelsolin family genes in zebrafish: a novel scinderin-like gene (scinla) encodes the major corneal crystallin.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2007
    Article
  13. Article
  14. Review
  15. Article
  16. Article
  17. Article
  18. Phosphatidylinositol 4,5-bisphosphate modifies tubulin participation in phospholipase Cbeta1 signaling.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2002
    Article
  19. Sparks and puffs in oligodendrocyte progenitors: cross talk between ryanodine receptors and inositol trisphosphate receptors.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2001
    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

3 authors at 1 institution in 1 country.

H q SunDepartment of Physiology, University of Texas Southwestern Medical Center at Dallas 75235-9040, USA.
K m Lin
H L Yin
The University of Texas Southwestern Medical Center · US

Funding

STRUCTURE/FUNCTION ANALYSIS OF CYTOPLASMIC GELSOLINR01GM051112 · NIGMS · UNIVERSITY OF TEXAS SW MED CTR/DALLAS · PI YIN, HELEN L · 1994 to 2003
$1.2M
NIGMS NIH HHS GM51112
6 · The paper itself

Abstract

Gelsolin and CapG are actin regulatory proteins that remodel the cytoskeleton in response to phosphatidylinositol 4,5-bisphosphate (PIP2) and Ca2+ during agonist stimulation. A physiologically relevant rise in Ca2+ increases their affinity for PIP2 and can promote significant interactions with PIP2 in activated cells. This may impact divergent PIP2- dependent signaling processes at the level of substrate availability. We found that CapG overexpression enhances PDGF-stimulated phospholipase Cgamma (PLCgamma) activity (Sun, H.-q., K. Kwiatkowska, D.C. Wooten, and H.L. Yin. 1995. J. Cell Biol. 129:147-156). In this paper, we examined the ability of gelsolin and CapG to compete with another PLC for PIP2 in live cells, in semiintact cells, and in vitro. We found that CapG and gelsolin overexpression profoundly inhibited bradykinin-stimulated PLCbeta. Inhibition occurred at or after the G protein activation step because overexpression also reduced the response to direct G protein activation with NaF. Bradykinin responsiveness was restored after cytosolic proteins, including gelsolin, leaked out of the overexpressing cells. Conversely, exogenous gelsolin added to permeabilized cells inhibited response in a dose-dependent manner. The washout and addback experiments clearly establish that excess gelsolin is the primary cause of PLC inhibition in cells. In vitro experiments showed that gelsolin and CapG stimulated as well as inhibited PLCbeta, and only gelsolin domains containing PIP2-binding sites were effective. Inhibition was mitigated by increasing PIP2 concentration in a manner consistent with competition between gelsolin and PLCbeta for PIP2. Gelsolin and CapG also had biphasic effects on tyrosine kinase- phosphorylated PLCgamma, although they inhibited PLCgamma less than PLCbeta. Our findings indicate that as PIP2 level and availability change during signaling, cross talk between PIP2-regulated proteins provides a selective mechanism for positive as well as negative regulation of the signal transduction cascade.

Indexed as

3T3 CellsAnimalsBacterial ProteinsBradykininCalciumCell Membrane PermeabilityClone CellsEnzyme ActivationGelsolinHydrolysisMiceMicrofilament ProteinsNuclear ProteinsPhosphatidylinositol 4,5-DiphosphatePhospholipidsProtein BindingBacterial ProteinsBradykininCalciumCapg protein, mouseGelsolinMicrofilament ProteinsNuclear ProteinsPhosphatidylinositol 4,5-DiphosphatePhospholipidsstreptolysin OStreptolysinsType C Phospholipases

Identifiers

PMID9265648
PMCPMC2138049
OpenAlexW2166928150

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
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.