Evidence map›Paper›PMID 15194810›Full record

ArticleMolecular biology of the cell2004

Identification of integrin beta subunit mutations that alter heterodimer function in situ.

Alison L Jannuzi, Thomas A Bunch, Robert F West, Danny L Brower

Abstract read
In one paragraph

Article in Molecular biology of the cell, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing 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

20 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Review
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
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  11. Article
  12. Article
  13. Analysis of conserved residues in the betapat-3 cytoplasmic tail reveals important functions of integrin in multiple tissues.Developmental dynamics : an official publication of the American Association of Anatomists · 2010
    Article
  14. Presynaptic secretion of mind-the-gap organizes the synaptic extracellular matrix-integrin interface and postsynaptic environments.Developmental dynamics : an official publication of the American Association of Anatomists · 2009
    Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. Integrin structures and conformational signaling.Current opinion in cell biology · 2006
    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

4 authors.

Alison L JannuziDepartment of Molecular and Cellular Biology, Arizona Cancer Center, University of Arizona, Tucson, Arizona 85724, USA.
Thomas A Bunch
Robert F West
Danny L Brower

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

We conducted a genetic screen for mutations in myospheroid, the gene encoding the Drosophila betaPS integrin subunit, and identified point mutants in all of the structural domains of the protein. Surprisingly, we find that mutations in very strongly conserved residues will often allow sufficient integrin function to support the development of adult animals, including mutations in the ADMIDAS site and in a cytoplasmic NPXY motif. Many mutations in the I-like domain reduce integrin expression specifically when betaPS is combined with activating alphaPS2 cytoplasmic mutations, indicating that integrins in the extended conformation are unstable relative to the inactive, bent heterodimers. Interestingly, the screen has identified alleles that show gain-of-function characteristics in cell culture, but have negative effects on animal development or viability. This is illustrated by the allele mys(b58); available structural models suggest that the molecular lesion of mys(b58), V409>D, should promote the "open" conformation of the beta subunit I-like domain. This expectation is supported by the finding that alphaPS2betaPS (V409>D) promotes adhesion and spreading of S2 cells more effectively than does wild-type alphaPS2betaPS, even when betaPS is paired with alphaPS2 containing activating cytoplasmic mutations. Finally, comparisons with the sequence of human beta8 suggest that evolution has targeted the "mys(b58)" residue as a means of affecting integrin activity.

Indexed as

AllelesAmino Acid MotifsAmino Acid SequenceAnimalsCell AdhesionCell MovementDrosophilaDrosophila ProteinsEpitheliumGenetic TestingIntegrin alpha ChainsIntegrin beta ChainsIntegrinsMolecular Sequence DataPoint MutationProtein Structure, TertiaryDrosophila Proteinsif protein, DrosophilaIntegrin alpha ChainsIntegrin beta ChainsIntegrins

Identifiers

PMID15194810
PMCPMC491840

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.