Evidence map›Paper›PMID 18347014›Full record

ArticleThe Journal of biological chemistry2008

Dematin and adducin provide a novel link between the spectrin cytoskeleton and human erythrocyte membrane by directly interacting with glucose transporter-1.

Anwar A Khan, Toshihiko Hanada, Morvarid Mohseni, Jong-Jin Jeong, Lixiao Zeng, Massimiliano Gaetani, Donghai Li, Brent C Reed, David W Speicher, Athar H Chishti

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 49 papers.

0numbers the graph read from it
0cells of the map it votes in
49citing papers in PubMed
4.1field-weighted citation impact, top 6% 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

49 citing papers in PubMed, 88 citations in OpenAlex.

  1. Trial
  2. Direct targeting of GLUT1 in cancer: A decade of inhibitor discovery and medicinal chemistry insights.Medicinal chemistry research : an international journal for rapid communications on design and mechanisms of action of biologically active agents · 2026
    Review
  3. Article
  4. Article
  5. [Effect of deletion of protein 4.1R on proliferation, apoptosis and glycolysis of hepatocyte HL-7702 cells].Nan fang yi ke da xue xue bao = Journal of Southern Medical University · 2024
    Article
  6. Article
  7. Review
  8. Review
  9. Article
  10. Article
  11. Review
  12. Erythroid glucose transport in health and disease.Pflugers Archiv : European journal of physiology · 2020
    Review
  13. Article
  14. QTL Analysis of Resistance to High-Intensity UV-B Irradiation in Soybean (International journal of molecular sciences · 2019
    Article
  15. Red cell membrane proteins.HemaSphere · 2019
    Article
  16. Article
  17. Review
  18. Article
  19. Review
  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

10 authors at 5 institutions in 1 country.

Anwar A KhanDepartment of Pharmacology, University of Illinois Cancer Center, University of Illinois College of Medicine, Chicago, IL 60612, USA.
Toshihiko Hanada
Morvarid Mohseni
Jong-Jin Jeong
Lixiao Zeng
Massimiliano Gaetani
Donghai Li
Brent C Reed
David W Speicher
Athar H Chishti
The Wistar Institute · USUniversity of Illinois Urbana-Champaign · USUniversity of Illinois Chicago · USIllinois College · USLouisiana State University Health Sciences Center Shreveport · US

Funding

Membrane Proteins of Normal and Abnormal Red CellsR01HL038794 · NHLBI · WISTAR INSTITUTE · PI SPEICHER, DAVID W. · 1987 to 2013
$5.1M
FUNCTIONAL STUDIES OF RED BLOOD CELL DEMATINR01HL051445 · NHLBI · UNIVERSITY OF ILLINOIS AT CHICAGO · PI CHISHTI, ATHAR H. · 1994 to 2010
$1.9M
Functional Studies of Erythrocyte DematinR56HL051445 · NHLBI · UNIVERSITY OF ILLINOIS AT CHICAGO · PI CHISHTI, ATHAR H. · 2008 to 2008
$393k
NHLBI NIH HHS HL 051445NHLBI NIH HHS HL 38794NHLBI NIH HHS R01 HL038794
6 · The paper itself

Abstract

Dematin and adducin are actin-binding proteins located at the spectrin-actin junctions, also called the junctional complex, in the erythrocyte membrane. Here we propose a new model whereby dematin and adducin link the junctional complex to human erythrocyte plasma membrane. Using a combination of surface labeling, immunoprecipitation, and vesicle proteomics approaches, we have identified glucose transporter-1 as the receptor for dematin and adducin in the human erythrocyte membrane. This finding is the first description of a transmembrane protein that binds to dematin and adducin, thus providing a rationale for the attachment of the junctional complex to the lipid bilayer. Because homologues of dematin, adducin, and glucose transporter-1 exist in many non-erythroid cells, we propose that a conserved mechanism may exist that couples sugar and other related transporters to the actin cytoskeleton.

Indexed as

AdducinsAnimalsBlood ProteinsCalmodulin-Binding ProteinsCell LineCytoskeletonErythrocyte MembraneGlucose Transporter Type 1HumansMiceProtein BindingProteomicsAdducinsBlood ProteinsCalmodulin-Binding ProteinsGlucose Transporter Type 1

Identifiers

PMID18347014
PMCPMC2386908
OpenAlexW1981209755

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.