Evidence map›Paper›PMID 19176526›Full record

ArticleThe Journal of biological chemistry2009

Role of phosphorylation and basic residues in the catalytic domain of cytosolic phospholipase A2alpha in regulating interfacial kinetics and binding and cellular function.

Dawn E Tucker, Moumita Ghosh, Farideh Ghomashchi, Robyn Loper, Saritha Suram, Bonnie St John, Milena Girotti, James G Bollinger, Michael H Gelb, Christina C Leslie

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.

0numbers the graph read from it
0cells of the map it votes in
26citing papers in PubMed
3.0field-weighted citation impact, top 9% 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

26 citing papers in PubMed, 53 citations in OpenAlex.

  1. Phospholipases: Where Do We Stand?Methods in molecular biology (Clifton, N.J.) · 2027
    Review
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  15. A stochastic signaling network mediates the probabilistic induction of cerebellar long-term depression.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2012
    Article
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  18. Review
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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

10 authors at 4 institutions in 1 country.

Dawn E TuckerProgram in Cell Biology, Department of Pediatrics, National Jewish Health, Denver, Colorado 80206, USA.
Moumita Ghosh
Farideh Ghomashchi
Robyn Loper
Saritha Suram
Bonnie St John
Milena Girotti
James G Bollinger
Michael H Gelb
Christina C Leslie
National Jewish Health · USUniversity of Washington · USUniversity of Colorado Denver · USUniversity of Colorado Boulder · US

Funding

TRANSLOCATION AND TRANSCELLULAR BIOSYNTHESISP01HL034303 · NHLBI · NATIONAL JEWISH HEALTH · PI BRATTON, DONNA L · 1985 to 2015
$25.0M
REGULATION OF PHOSPHOLIPASE A2 NUCLEAR TARGETINGR01HL061378 · NHLBI · NATIONAL JEWISH HEALTH · PI LESLIE, CHRISTINA CARROLL · 1999 to 2011
$4.1M
Regulation and Function of Cytosolic Phospholipase A2R01HL050040 · NHLBI · UNIVERSITY OF WASHINGTON · PI GELB, MICHAEL H · 1993 to 2012
$2.4M
NHLBI NIH HHS HL34303NHLBI NIH HHS HL50040NHLBI NIH HHS HL61378NHLBI NIH HHS P01 HL034303NHLBI NIH HHS R01 HL050040NHLBI NIH HHS R01 HL061378
6 · The paper itself

Abstract

Group IVA cytosolic phospholipase A(2) (cPLA(2)alpha) is regulated by phosphorylation and calcium-induced translocation to membranes. Immortalized mouse lung fibroblasts lacking endogenous cPLA(2)alpha (IMLF(-/-)) were reconstituted with wild type and cPLA(2)alpha mutants to investigate how calcium, phosphorylation, and the putative phosphatidylinositol 4,5-bisphosphate (PIP(2)) binding site regulate translocation and arachidonic acid (AA) release. Agonists that elicit distinct modes of calcium mobilization were used. Serum induced cPLA(2)alpha translocation to Golgi within seconds that temporally paralleled the initial calcium transient. However, the subsequent influx of extracellular calcium was essential for stable binding of cPLA(2)alpha to Golgi and AA release. In contrast, phorbol 12-myristate 13-acetate induced low amplitude calcium oscillations, slower translocation of cPLA(2)alpha to Golgi, and much less AA release, which were blocked by chelating extracellular calcium. AA release from IMLF(-/-) expressing phosphorylation site (S505A) and PIP(2) binding site (K488N/K543N/K544N) mutants was partially reduced compared with cells expressing wild type cPLA(2)alpha, but calcium-induced translocation was not impaired. Consistent with these results, Ser-505 phosphorylation did not change the calcium requirement for interfacial binding and catalysis in vitro but increased activity by 2-fold. Mutations in basic residues in the catalytic domain of cPLA(2)alpha reduced activation by PIP(2) but did not affect the concentration of calcium required for interfacial binding or phospholipid hydrolysis. The results demonstrate that Ser-505 phosphorylation and basic residues in the catalytic domain principally act to regulate cPLA(2)alpha hydrolytic activity.

Indexed as

Catalytic DomainAnimalsCalciumCells, CulturedCulture Media, Serum-FreeEnzyme ActivationGene Expression RegulationGroup IV Phospholipases A2HumansKineticsMiceMice, KnockoutMutationPhosphorylationProtein BindingProtein TransportCalciumCulture Media, Serum-FreeGroup IV Phospholipases A2phorbolol myristate acetateTetradecanoylphorbol Acetate

Identifiers

PMID19176526
PMCPMC2666612
OpenAlexW1999045066

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.