Evidence map›Paper›PMID 18674540›Full record

ArticleJournal of molecular biology2008

Specific heteromeric association of four transmembrane peptides derived from platelet glycoprotein Ib-IX complex.

Shi-Zhong Luo, Renhao Li

Open access · greenAbstract read
In one paragraph

Article in Journal of molecular biology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing 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

20 citing papers in PubMed, 31 citations in OpenAlex.

  1. Review
  2. Article
  3. Structure-function of platelet glycoprotein Ib-IX.Journal of thrombosis and haemostasis : JTH · 2020
    Review
  4. Article
  5. Article
  6. Review
  7. Article
  8. Membrane-enabled dimerization of the intrinsically disordered cytoplasmic domain of ADAM10.Proceedings of the National Academy of Sciences of the United States of America · 2014
    Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. The organizing principle of the platelet glycoprotein Ib-IX-V complex.Journal of thrombosis and haemostasis : JTH · 2013
    Review
  14. Article
  15. Article
  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

2 authors at 1 institution in 1 country.

Shi-Zhong LuoCenter for Membrane Biology, Department of Biochemistry and Molecular Biology, The University of Texas Health Science Center at Houston, Houston, TX 77030, USA.
Renhao Li
The University of Texas Health Science Center at Houston · US

Funding

Structure and Function of Platelet Glycoprotein lb-IX-V ComplexR01HL082808 · NHLBI · UNIVERSITY OF TEXAS HLTH SCI CTR HOUSTON · PI LI, RENHAO · 2006 to 2023
$6.4M
NHLBI NIH HHS HL082808NHLBI NIH HHS R01 HL082808
6 · The paper itself

Abstract

As the receptor on the platelet surface for von Willebrand factor, glycoprotein (GP) Ib-IX complex is critically involved in hemostasis and thrombosis. How the complex is assembled from GP Ibalpha, GP Ib beta and GP IX subunits, all of which are type I transmembrane proteins, is not entirely clear. Genetic and mutational analyses have identified the transmembrane (TM) domains of these subunits as active participants in assembly of the complex. In this study, peptides containing the transmembrane domain of each subunit have been produced and their interaction with one another characterized. Only the Ib beta TM sequence, but not the Ibalpha and IX counterparts, can form homo-oligomers in SDS-PAGE and TOXCAT assays. Following up on our earlier observation that a Ib beta-Ibalpha-Ib beta peptide complex (alphabeta(2)) linked through native juxtamembrane disulfide bonds could be produced from isolated Ibalpha and Ib beta TM peptides in detergent micelles, we show here that addition of the IX TM peptide facilitates formation of the native alphabeta(2) complex, reproducing the same effect by the IX subunit in cells expressing the GP Ib-IX complex. Specific fluorescence resonance energy transfer was observed between donor-labeled alphabeta(2) peptide complex and acceptor-conjugated IX TM peptide in micelles. Finally, the mutation D135K in the IX TM peptide could hamper both the formation of the alphabeta(2) complex and the energy transfer, consistent with its reported effect in the full-length complex. Overall, our results have demonstrated directly the native-like heteromeric interaction among the isolated Ibalpha, Ib beta and IX TM peptides, which provides support for the four-helix bundle model of the TM domains in the GP Ib-IX complex and paves the way for further structural analysis. The methods developed in this study may be applicable to other studies of heteromeric interaction among multiple TM helices.

Indexed as

Protein Structure, QuaternaryAmino Acid SequenceAnimalsBlood PlateletsCell LineCell MembraneDetergentsDisulfidesFluorescence Resonance Energy TransferMicellesModels, MolecularMolecular Sequence DataPeptidesPlatelet Glycoprotein GPIb-IX ComplexSequence AlignmentSulfhydryl CompoundsDetergentsDisulfidesMicellesPeptidesPlatelet Glycoprotein GPIb-IX ComplexSulfhydryl Compounds

Identifiers

PMID18674540
PMCPMC2563799
OpenAlexW2007456791

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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.