Evidence map›Paper›PMID 20433199›Full record

ArticleBiochemistry2010

Control of erythrocyte membrane-skeletal cohesion by the spectrin-membrane linkage.

Lionel Blanc, Marcela Salomao, Xinhua Guo, Xiuli An, Walter Gratzer, Narla Mohandas

Abstract read
In one paragraph

Article in Biochemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
–field-weighted citation impact
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

21 citing papers in PubMed.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Multiple Functions of Spectrin: Convergent Effects.The Journal of membrane biology · 2020
    Review
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. Review
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

6 authors.

Lionel BlancRed Cell Physiology Laboratory, New York Blood Center, New York, New York 10065, USA. LBlanc@NYBloodCenter.org
Marcela Salomao
Xinhua Guo
Xiuli An
Walter Gratzer
Narla Mohandas

Funding

YEAST MEMBRANE CYTOSKELETONP01DK032094 · NIDDK · UNIVERSITY OF CALIFORNIA SAN FRANCISCO · PI NARLA, MOHANDAS · 1987 to 2021
$26.7M
RED CELL DEFORMABILITY IN VITRO AND SURVIVAL IN VIVOR37DK026263 · NIDDK · UNIVERSITY OF CALIF-LAWRENC BERKELEY LAB · PI NARLA, MOHANDAS · 1995 to 2017
$4.5M
RHEOLOGICAL AND ADHERENCE PROPERTIES OF SICKLE CELLSR01HL031579 · NHLBI · UNIVERSITY OF CALIFORNIA SAN FRANCISCO · PI NARLA, MOHANDAS · 1985 to 2010
$3.8M
RED CELL DEFORMABILITY IN VITRO AND SURVIVAL IN VIVOR01DK026263 · NIDDK · UNIVERSITY OF CALIFORNIA SAN FRANCISCO · PI NARLA, MOHANDAS · 1986 to 2007
$1.6M
NHLBI NIH HHS HL31579NHLBI NIH HHS R01 HL031579NIDDK NIH HHS DK26263NIDDK NIH HHS DK32094NIDDK NIH HHS P01 DK032094NIDDK NIH HHS R01 DK026263NIDDK NIH HHS R37 DK026263
6 · The paper itself

Abstract

Spectrin tetramer is the major structural member of the membrane-associated skeletal network of red cells. We show here that disruption of the spectrin-ankyrin-band 3 link to the membrane leads to dissociation of a large proportion of the tetramers into dimers. Noncovalent perturbation of the linkage was induced by a peptide containing the ankyrin-binding site of the spectrin beta-chain, and covalent perturbation by treatment with the thiol reagent, N-ethylmaleimide (NEM). This reagent left the intrinsic self-association capacity of the spectrin dimers unaffected and disturbed only the ankyrin-band 3 interaction. The dissociation of spectrin tetramers on the membrane into functional dimers was confirmed by the binding of a spectrin peptide directed against the self-association sites. Dissociation of the tetramers resulted, we infer, from detachment of the proximal ends of the constituent dimers from the membrane, thereby reducing their proximity to one another and thus weakening their association. The measured affinity of the interaction of the peptides with the free dimer ends on the membrane permits an estimate of the equilibrium between intact and dissociated tetramers on the native membrane. This indicates that in the physiological state the equilibrium proportion of the dissociated tetramers may be as high as 5-10%. These findings enabled us to identify an additional important functional role for the spectrin-ankyrin-band 3 link in regulating spectrin self-association in the red cell membrane.

Indexed as

AnkyrinsBinding SitesCell MembraneCellular StructuresCytoskeletonErythrocyte MembraneErythrocytesEthylmaleimideMusculoskeletal SystemPhysical PhenomenaProtein BindingSpectrinAnkyrinsEthylmaleimideSpectrin

Identifiers

PMID20433199
PMCPMC3056085

What OpenQuestion holds

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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.