Evidence map›Paper›PMID 26271157›Full record

ArticleJournal of proteomics2015

Proteome analysis of the triton-insoluble erythrocyte membrane skeleton.

Avik Basu, Sandra Harper, Esther N Pesciotta, Kaye D Speicher, Abhijit Chakrabarti, David W Speicher

Abstract read
In one paragraph

Article in Journal of proteomics, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.

0numbers the graph read from it
0cells of the map it votes in
10citing 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

10 citing papers in PubMed.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Myosin IIA interacts with the spectrin-actin membrane skeleton to control red blood cell membrane curvature and deformability.Proceedings of the National Academy of Sciences of the United States of America · 2018
    Article
  9. Article
  10. 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

6 authors.

Avik BasuThe Center for Systems and Computational Biology and Molecular and Cellular Oncogenesis Program, The Wistar Institute, Philadelphia, PA, USA; Crystallography and Molecular Biology Division, Saha Institute of Nuclear Physics, Kolkata, India.
Sandra HarperThe Center for Systems and Computational Biology and Molecular and Cellular Oncogenesis Program, The Wistar Institute, Philadelphia, PA, USA.
Esther N PesciottaThe Center for Systems and Computational Biology and Molecular and Cellular Oncogenesis Program, The Wistar Institute, Philadelphia, PA, USA; Department of Pediatrics, Children's Hospital of Philadelphia, Philadelphia, PA, USA.
Kaye D SpeicherThe Center for Systems and Computational Biology and Molecular and Cellular Oncogenesis Program, The Wistar Institute, Philadelphia, PA, USA.
Abhijit ChakrabartiCrystallography and Molecular Biology Division, Saha Institute of Nuclear Physics, Kolkata, India.
David W SpeicherThe Center for Systems and Computational Biology and Molecular and Cellular Oncogenesis Program, The Wistar Institute, Philadelphia, PA, USA. Electronic address: speicher@wistar.org.

Funding

Tumor Microenvironment and MetastasisP30CA010815 · NCI · WISTAR INSTITUTE · PI Luis J Montaner · 1985 to 2026
$75.9M
HEMATOPOIESIS TRAINING GRANTT32DK007780 · NIDDK · UNIVERSITY OF PENNSYLVANIA · PI TONG, WEI · 1999 to 2023
$6.7M
Membrane Proteins of Normal and Abnormal Red CellsR01HL038794 · NHLBI · WISTAR INSTITUTE · PI SPEICHER, DAVID W. · 1987 to 2013
$5.1M
CHANGES IN THE RBC PROTEOME DURING HEALTH AND DISEASER01DK084188 · NIDDK · CHILDREN'S HOSP OF PHILADELPHIA · PI ABDULMALIK, OSHEIZA Y · 2010 to 2014
$2.0M
NCI NIH HHS P30 CA010815NHLBI NIH HHS R01 HL038794NIDDK NIH HHS R01 DK084188
6 · The paper itself

Abstract

Erythrocyte shape and membrane integrity is imparted by the membrane skeleton, which can be isolated as a Triton X-100 insoluble structure that retains the biconcave shape of intact erythrocytes, indicating isolation of essentially intact membrane skeletons. These erythrocyte "Triton Skeletons" have been studied morphologically and biochemically, but unbiased proteome analysis of this substructure of the membrane has not been reported. In this study, different extraction buffers and in-depth proteome analyses were used to more fully define the protein composition of this functionally critical macromolecular complex. As expected, the major, well-characterized membrane skeleton proteins and their associated membrane anchors were recovered in good yield. But surprisingly, a substantial number of additional proteins that are not considered in erythrocyte membrane skeleton models were recovered in high yields, including myosin-9, lipid raft proteins (stomatin, flotillin1 and 2), multiple chaperone proteins (HSPs, protein disulfide isomerase and calnexin), and several other proteins. These results show that the membrane skeleton is substantially more complex than previous biochemical studies indicated, and it apparently has localized regions with unique protein compositions and functions. This comprehensive catalog of the membrane skeleton should lead to new insights into erythrocyte membrane biology and pathogenic mutations that perturb membrane stability. Biological significance Current models of erythrocyte membranes describe fairly simple homogenous structures that are incomplete. Proteome analysis of the erythrocyte membrane skeleton shows that it is quite complex and includes a substantial number of proteins whose roles and locations in the membrane are not well defined. Further elucidation of interactions involving these proteins and definition of microdomains in the membrane that contain these proteins should yield novel insights into how the membrane skeleton produces the normal biconcave erythrocyte shape and how it is perturbed in pathological conditions that destabilize the membrane.

Indexed as

Cells, CulturedErythrocyte MembraneHumansMembrane MicrodomainsMembrane ProteinsOctoxynolProteomeSolubilityMembrane ProteinsOctoxynolProteomeErythrocytesMembrane compositionMembrane skeletonMembrane structureProteomicsTriton Skeleton

Identifiers

PMID26271157
PMCPMC4619114

What OpenQuestion holds

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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.