Evidence map›Paper›PMID 23696644›Full record

ArticleThe Journal of biological chemistry2013

Drebrin-induced stabilization of actin filaments.

Mouna A Mikati, Elena E Grintsevich, Emil Reisler

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 40 papers.

0numbers the graph read from it
0cells of the map it votes in
40citing papers in PubMed
3.7field-weighted citation impact, top 7% 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

40 citing papers in PubMed, 90 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Article
  5. Article
  6. Article
  7. Unraveling a Key Molecular Player Governing Pulmonary Alveolar Development.American journal of respiratory cell and molecular biology · 2024
    Article
  8. Article
  9. Article
  10. Article
  11. Drebrin, an actin-binding protein, is required for lens morphogenesis and growth.Developmental dynamics : an official publication of the American Association of Anatomists · 2021
    Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Review
  17. Progranulin/EphA2 axis: A novel oncogenic mechanism in bladder cancer.Matrix biology : journal of the International Society for Matrix Biology · 2020
    Article
  18. Review
  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

3 authors at 1 institution in 1 country.

Mouna A MikatiDepartment of Chemistry and Biochemistry, of California Los Angeles, Los Angeles, California 90095, USA.
Elena E Grintsevich
Emil Reisler
University of California, Los Angeles · US

Funding

Dynamic Events in Myosin and Actin and Their FunctionR01GM077190 · NIGMS · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI REISLER, EMIL · 2006 to 2020
$6.2M
HIGH-END CRYOEM INSTRUMENT FOR UCLA ELECTRON IMAGING CTR FOR NANOMACHINES: AIDSS10RR023057 · NCRR · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI ZHOU, Z HONG · 2006 to 2006
$1.6M
NCRR NIH HHS S10 RR023057NIGMS NIH HHS R01 GM077190
6 · The paper itself

Abstract

Drebrin is a mammalian neuronal protein that binds to and organizes filamentous actin (F-actin) in dendritic spines, the receptive regions of most excitatory synapses that play a crucial role in higher brain functions. Here, the structural effects of drebrin on F-actin were examined in solution. Depolymerization and differential scanning calorimetry assays show that F-actin is stabilized by the binding of drebrin. Drebrin inhibits depolymerization mainly at the barbed end of F-actin. Full-length drebrin and its C-terminal truncated constructs were used to clarify the domain requirements for these effects. The actin binding domain of drebrin decreases the intrastrand disulfide cross-linking of Cys-41 (in the DNase I binding loop) to Cys-374 (C-terminal) but increases the interstrand disulfide cross-linking of Cys-265 (hydrophobic loop) to Cys-374 in the yeast mutants Q41C and S265C, respectively. We also demonstrate, using solution biochemistry methods and EM, the rescue of filament formation by drebrin in different cases of longitudinal interprotomer contact perturbation: the T203C/C374S yeast actin mutant and grimelysin-cleaved skeletal actin (between Gly-42 and Val-43). Additionally, we show that drebrin rescues the polymerization of V266G/L267G, a hydrophobic loop yeast actin mutant with an impaired lateral interface formation between the two filament strands. Overall, our data suggest that drebrin stabilizes actin filaments through its effect on their interstrand and intrastrand contacts.

Indexed as

Amino Acid SubstitutionAnimalsMutation, MissenseNerve Tissue ProteinsNeuropeptidesProtein Structure, SecondaryRabbitsSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsStress FibersdrebrinsNerve Tissue ProteinsNeuropeptidesSaccharomyces cerevisiae ProteinsActinCytoskeletonElectron Microscopy (EM)Protein ComplexesProtein Cross-linkingProtein DynamicsProtein Stability

Identifiers

PMID23696644
PMCPMC3707693
OpenAlexW2124015317

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.