Evidence map›Paper›PMID 20670370›Full record

ArticleJournal of thrombosis and haemostasis : JTH2010

Differential phosphorylation of myosin light chain (Thr)18 and (Ser)19 and functional implications in platelets.

T M Getz, C A Dangelmaier, J Jin, J L Daniel, S P Kunapuli

Open access · greenAbstract read
In one paragraph

Article in Journal of thrombosis and haemostasis : JTH, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
1.6field-weighted citation impact, top 17% 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

22 citing papers in PubMed, 48 citations in OpenAlex.

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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

5 authors at 1 institution in 1 country.

T M GetzDepartment of Physiology, Temple University School of Medicine, Philadelphia, PA 19140, USA.
C A Dangelmaier
J Jin
J L Daniel
S P Kunapuli
Temple University · US

Funding

Training in Thrombosis, Hemostasis and Vascular BiologyT32HL007777 · NHLBI · TEMPLE UNIV OF THE COMMONWEALTH · PI KUNAPULI, SATYA P. · 1993 to 2012
$5.2M
MOLECULAR BASIS FOR ADP INDUCED PLATELET ACTIVATIONR01HL060683 · NHLBI · TEMPLE UNIV OF THE COMMONWEALTH · PI KUNAPULI, SATYA P. · 1998 to 2011
$3.9M
Functional PKC Isoforms in PlateletsR01HL093231 · NHLBI · TEMPLE UNIV OF THE COMMONWEALTH · PI KUNAPULI, SATYA P. · 2009 to 2017
$3.6M
Functional G Protein pathways in platelet activationR01HL081322 · NHLBI · TEMPLE UNIV OF THE COMMONWEALTH · PI KUNAPULI, SATYA P. · 2006 to 2010
$2.9M
Platelet ADP ReceptorsR01HL080444 · NHLBI · TEMPLE UNIV OF THE COMMONWEALTH · PI KUNAPULI, SATYA P. · 2005 to 2008
$1.8M
NHLBI NIH HHS HL07777NHLBI NIH HHS HL60683NHLBI NIH HHS HL80444NHLBI NIH HHS HL81322NHLBI NIH HHS R01 HL060683NHLBI NIH HHS R01 HL080444NHLBI NIH HHS R01 HL081322NHLBI NIH HHS R01 HL093231NHLBI NIH HHS T32 HL007777
6 · The paper itself

Abstract

backgroundMyosin IIA is an essential platelet contractile protein that is regulated by phosphorylation of its regulatory light chain (MLC) on residues (Thr)18 and (Ser)19 via the myosin light chain kinase (MLCK).

objectiveThe present study was carried out to elucidate the mechanisms regulating MLC (Ser)19 and (Thr)18 phosphorylation and the functional consequence of each phosphorylation event in platelets.

resultsInduction of 2MeSADP-induced shape change occurs within 5s along with robust phosphorylation of MLC (Ser)19 with minimal phosphorylation of MLC (Thr)18. Selective activation of G(12/13) produces both slow shape change and comparably slow MLC (Thr)18 and (Ser)19 phosphorylation. Stimulation with agonists that trigger ATP secretion caused rapid MLC (Ser)19 phosphorylation while MLC (Thr)18 phosphorylation was coincident with secretion. Platelets treated with p160(ROCK) inhibitor Y-27632 exhibited a partial inhibition in secretion and had a substantial inhibition in MLC (Thr)18 phosphorylation without effecting MLC (Ser)19 phosphorylation. These data suggest that phosphorylation of MLC (Ser)19 is downstream of Gq/Ca(2+) -dependent mechanisms and sufficient for shape change, whereas MLC (Thr)18 phosphorylation is substantially downstream of G(12/13) -regulated Rho kinase pathways and necessary, probably in concert with MLC (Ser)19 phosphorylation, for full contractile activity leading to dense granule secretion. Overall, we suggest that the amplitude of the platelet contractile response is differentially regulated by a least two different signaling pathways, which lead to different phosphorylation patterns of the myosin light chain, and this mechanism results in a graded response rather than a simple on/off switch.

Indexed as

Adenosine DiphosphateBlood PlateletsCalciumCell ShapeHumansKineticsMyosin Light ChainsPhosphorylationPlatelet Aggregationrho-Associated KinasesSerineSignal TransductionThreonineAdenosine DiphosphateCalciumMyosin Light Chainsrho-Associated KinasesSerineThreonine

Identifiers

PMID20670370
PMCPMC2965805
OpenAlexW1507708600

What OpenQuestion holds

Textmetadata
LicenceTDM
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.