Evidence map›Paper›PMID 18287096›Full record

ArticleThe Journal of biological chemistry2008

Unexpected complexity in the mechanisms that target assembly of the spectrin cytoskeleton.

Amlan Das, Christine Base, Debasis Manna, Wonhwa Cho, Ronald R Dubreuil

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 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
1.7field-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

18 citing papers in PubMed, 34 citations in OpenAlex.

  1. Article
  2. Article
  3. α-Synuclein Promotes Neuronal Dysfunction and Death by Disrupting the Binding of Ankyrin to β-Spectrin.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2023
    Article
  4. Article
  5. Review
  6. Article
  7. Article
  8. Article
  9. Article
  10. Review
  11. Article
  12. Nesprins: from the nuclear envelope and beyond.Expert reviews in molecular medicine · 2013
    Review
  13. Article
  14. Review
  15. Review
  16. Article
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  18. 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

5 authors at 2 institutions in 2 countries.

Amlan DasLaboratory for Molecular Biology and Department of Biological Sciences, University of Illinois, Chicago, Illinois 60607, USA.
Christine Base
Debasis Manna
Wonhwa Cho
Ronald R Dubreuil
Laboratory of Molecular Genetics · PLUniversity of Illinois Chicago · US

Funding

Membrane Targeting by Phosphoinositide-Binding ProteinsR01GM068849 · NIGMS · UNIVERSITY OF ILLINOIS AT CHICAGO · PI CHO, WONHWA · 2003 to 2015
$3.9M
GENETIC STUDIES OF THE MEMBRANE SKELETONR01GM049301 · NIGMS · UNIVERSITY OF ILLINOIS AT CHICAGO · PI DUBREUIL, RONALD R · 1995 to 2004
$1.1M
NIGMS NIH HHS GM49301NIGMS NIH HHS GM68849
6 · The paper itself

Abstract

The spectrin cytoskeleton assembles within discrete regions of the plasma membrane in a wide range of animal cell types. Although recent studies carried out in vertebrate systems indicate that spectrin assembly occurs indirectly through the adapter protein ankyrin, recent studies in Drosophila have established that spectrin can also assemble through a direct ankyrin-independent mechanism. Here we tested specific regions of the spectrin molecule for a role in polarized assembly and function. First, we tested mutant beta-spectrins lacking ankyrin binding activity and/or the COOH-terminal pleckstrin homology (PH) domain for their assembly competence in midgut, salivary gland, and larval brain. Remarkably, three different assembly mechanisms operate in these three cell types: 1) neither site was required for assembly in salivary gland; 2) only the PH domain was required in midgut copper cells; and 3) either one of the two sites was sufficient for spectrin assembly in larval brain. Further characterization of the PH domain revealed that it binds strongly to lipid mixtures containing phosphatidylinositol 4,5-bisphosphate (PIP(2)) but not phosphatidylinositol 3,4,5-trisphosphate. A K8Q mutation in the lipid binding region of the PH domain eliminated the PIP(2) interaction in vitro, yet the mutant protein retained full biological function in vivo. Reporter gene studies revealed that PIP(2) and the spectrin PH domain codistribute with one another in cells but not with authentic wild type alphabeta-spectrin. Thus, it appears that the PH domain imparts membrane targeting activity through a second mechanism that takes precedence over its PIP(2) binding activity.

Indexed as

AnimalsAnkyrinsBrainCell MembraneCytoskeletonDrosophila melanogasterImmunoprecipitationLarvaModels, BiologicalPhosphatidylinositol 4,5-DiphosphatePoint MutationProtein BindingProtein Structure, QuaternaryProtein Structure, TertiaryProtein TransportSalivary GlandsAnkyrinsPhosphatidylinositol 4,5-DiphosphateSpectrin

Identifiers

PMID18287096
PMCPMC2335364
OpenAlexW1969124533

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.