Evidence map›Paper›PMID 25381248›Full record

ArticleThe Journal of biological chemistry2015

Spectrin tetramer formation is not required for viable development in Drosophila.

Mansi R Khanna, Floyd J Mattie, Kristen C Browder, Megan D Radyk, Stephanie E Crilly, Katelyn J Bakerink, Sandra L Harper, David W Speicher, Graham H Thomas

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.

0numbers the graph read from it
0cells of the map it votes in
6citing papers in PubMed
0.7field-weighted citation impact, top 29% 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

6 citing papers in PubMed, 22 citations in OpenAlex.

  1. Article
  2. International journal of molecular sciences · 2021
    Review
  3. Article
  4. Article
  5. Article
  6. 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

9 authors at 2 institutions in 1 country.

Mansi R KhannaFrom the Department of Biology and the Department of Biochemistry and Molecular Biology, The Pennsylvania State University, University Park, Pennsylvania 16802 and.
Floyd J MattieFrom the Department of Biology and the Department of Biochemistry and Molecular Biology, The Pennsylvania State University, University Park, Pennsylvania 16802 and.
Kristen C BrowderFrom the Department of Biology and the Department of Biochemistry and Molecular Biology, The Pennsylvania State University, University Park, Pennsylvania 16802 and.
Megan D RadykFrom the Department of Biology and the Department of Biochemistry and Molecular Biology, The Pennsylvania State University, University Park, Pennsylvania 16802 and.
Stephanie E CrillyFrom the Department of Biology and the Department of Biochemistry and Molecular Biology, The Pennsylvania State University, University Park, Pennsylvania 16802 and.
Katelyn J BakerinkFrom the Department of Biology and the Department of Biochemistry and Molecular Biology, The Pennsylvania State University, University Park, Pennsylvania 16802 and.
Sandra L Harperthe Systems Biology Division, The Wistar Institute, Philadelphia, Pennsylvania 19104.
David W Speicherthe Systems Biology Division, The Wistar Institute, Philadelphia, Pennsylvania 19104.
Graham H ThomasFrom the Department of Biology and the Department of Biochemistry and Molecular Biology, The Pennsylvania State University, University Park, Pennsylvania 16802 and gxt5@psu.edu.
Pennsylvania State University · USThe Wistar Institute · US

Funding

Tumor Microenvironment and MetastasisP30CA010815 · NCI · WISTAR INSTITUTE · PI Luis J Montaner · 1985 to 2026
$75.9M
Membrane Proteins of Normal and Abnormal Red CellsR01HL038794 · NHLBI · WISTAR INSTITUTE · PI SPEICHER, DAVID W. · 1987 to 2013
$5.1M
NCI NIH HHS P30 CA010815NHLBI NIH HHS HL038794NHLBI NIH HHS R01 HL038794
6 · The paper itself

Abstract

The dominant paradigm for spectrin function is that (αβ)2-spectrin tetramers or higher order oligomers form membrane-associated two-dimensional networks in association with F-actin to reinforce the plasma membrane. Tetramerization is an essential event in such structures. We characterize the tetramerization interaction between α-spectrin and β-spectrins in Drosophila. Wild-type α-spectrin binds to both β- and βH-chains with high affinity, resembling other non-erythroid spectrins. However, α-spec(R22S), a tetramerization site mutant homologous to the pathological α-spec(R28S) allele in humans, eliminates detectable binding to β-spectrin and reduces binding to βH-spectrin ∼1000-fold. Even though spectrins are essential proteins, α-spectrin(R22S) rescues α-spectrin mutants to adulthood with only minor phenotypes indicating that tetramerization, and thus conventional network formation, is not the essential function of non-erythroid spectrin. Our data provide the first rigorous test for the general requirement for tetramer-based non-erythroid spectrin networks throughout an organism and find that they have very limited roles, in direct contrast to the current paradigm.

Indexed as

Actin CytoskeletonActinsAnimalsCell MembraneDrosophila melanogasterHumansMutationProtein MultimerizationSpectrinActinsSpectrinCell BiologyCytoskeletonDrosophilaMembrane ProteinMembrane SkeletonProtein AssemblySpectrin

Identifiers

PMID25381248
PMCPMC4294495
OpenAlexW2035759461

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.