Evidence map›Paper›PMID 10436021›Full record

ArticleMolecular biology of the cell1999

Regulation of F-actin binding to platelet moesin in vitro by both phosphorylation of threonine 558 and polyphosphatidylinositides.

F Nakamura, L Huang, K Pestonjamasp, E J Luna, H Furthmayr

Open access · greenAbstract read
In one paragraph

Article in Molecular biology of the cell, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 63 papers.

0numbers the graph read from it
0cells of the map it votes in
63citing papers in PubMed
6.7field-weighted citation impact, top 2% 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

63 citing papers in PubMed, 142 citations in OpenAlex.

  1. Review
  2. Article
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  4. Review
  5. Article
  6. ERM-1 Phosphorylation and NRFL-1 Redundantly Control Lumen Formation in theFrontiers in cell and developmental biology · 2022
    Article
  7. Article
  8. Article
  9. Article
  10. Review
  11. Review
  12. Review
  13. Article
  14. Article
  15. Article
  16. Article
  17. Review
  18. A glimpse of the ERM proteins.Journal of biomedical science · 2016
    Review
  19. Article
  20. Article

3 more citing papers are in PubMed but not listed here.

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 3 institutions in 2 countries.

F NakamuraLaboratory of Environmental Biochemistry, Department of Environmental Biology, Graduate School of Agricultural Sciences, Tohoku University, Sendai 981-8555, Japan.
L Huang
K Pestonjamasp
E J Luna
H Furthmayr
Stanford University · USUniversity of Massachusetts Chan Medical School · USTohoku University · JP

Funding

CYTOSKELTON-MEMBRANE INTERACTIONSR01GM033048 · NIGMS · WORCESTER FOUNDATION FOR BIOMEDICAL RES · PI LUNA, ELIZABETH J. · 1985 to 2009
$3.3M
METABOLISM OF THE DERMAL MICROVASCULAR BASEMENT MEMBRANEP01AR041045 · NIAMS · STANFORD UNIVERSITY · PI HERRON, G SCOTT · 1992 to 1996
–
NIAMS NIH HHS 1PO4-AR41045NIGMS NIH HHS GM-33048NIGMS NIH HHS R01 GM033048
6 · The paper itself

Abstract

Activation of human platelets with thrombin transiently increases phosphorylation at (558)threonine of moesin as determined with phosphorylation state-specific antibodies. This specific modification is completely inhibited by the kinase inhibitor staurosporine and maximally promoted by the phosphatase inhibitor calyculin A, making it possible to purify the two forms of moesin to homogeneity. Blot overlay assays with F-actin probes labeled with either [32P]ATP or 125I show that only phosphorylated moesin interacts with F-actin in total platelet lysates, in moesin antibody immunoprecipitates, and when purified. In the absence of detergents, both forms of the isolated protein are aggregated. Phosphorylated, purified moesin co-sediments with alpha- or beta/gamma-actin filaments in cationic, but not in anionic, nonionic, or amphoteric detergents. The interaction affinity is high (Kd, approximately 1.5 nM), and the maximal moesin:actin stoichiometry is 1:1. This interaction is also observed in platelets extracted with cationic but not with nonionic detergents. In 0.1% Triton X-100, F-actin interacts with phosphorylated moesin only in the presence of polyphosphatidylinositides. Thus, both polyphosphatidylinositides and phosphorylation can activate moesin's high-affinity F-actin binding site in vitro. Dual regulation by both mechanisms may be important for proper cellular control of moesin-mediated linkages between the actin cytoskeleton and the plasma membrane.

Indexed as

ActinsAmino Acid SequenceBiochemistryBlood PlateletsCytoskeletonDetergentsHumansMicrofilament ProteinsMolecular Sequence DataPhosphatidylinositol 4,5-DiphosphatePhosphatidylinositolsPhosphorylationQuaternary Ammonium CompoundsThreonineActinsDetergentsdodecyltrimethylammoniumMicrofilament ProteinsmoesinPhosphatidylinositol 4,5-DiphosphatePhosphatidylinositolsQuaternary Ammonium CompoundsThreonine

Identifiers

PMID10436021
PMCPMC25498
OpenAlexW2130436369

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.