Evidence map›Paper›PMID 18182012›Full record

ArticleTraffic (Copenhagen, Denmark)2008

Dynamitin mutagenesis reveals protein-protein interactions important for dynactin structure.

Kerstin C Maier, Jamie E Godfrey, Christophe J Echeverri, Frances K Y Cheong, Trina A Schroer

Open access · bronzeAbstract read
In one paragraph

Article in Traffic (Copenhagen, Denmark), 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
1.1field-weighted citation impact, top 24% 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

14 citing papers in PubMed, 25 citations in OpenAlex.

  1. Review
  2. Article
  3. VezA/vezatin facilitates proper assembly of the dynactin complex in vivo.bioRxiv : the preprint server for biology · 2024
    Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Dynactin function in mitotic spindle positioning.Traffic (Copenhagen, Denmark) · 2008
    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

5 authors at 2 institutions in 2 countries.

Kerstin C MaierDepartment of Biology, The Johns Hopkins University, 3400 North Charles Street, Baltimore, MD 21218, USA.
Jamie E Godfrey
Christophe J Echeverri
Frances K Y Cheong
Trina A Schroer
Johns Hopkins University · USCenix BioScience (Germany) · DE

Funding

REGULATION OF CYTOPLASMIC DYNEIN-BASED VESICLE TRANSPORTR01GM044589 · NIGMS · JOHNS HOPKINS UNIVERSITY · PI SCHROER, TRINA A · 1990 to 2012
$4.3M
MOLECULAR GENETICS OF CYTOPLASMIC DYNEINR37GM047434 · NIGMS · WORCESTER FOUNDATION FOR BIOMEDICAL RES · PI VALLEE, RICHARD BERT · 1996 to 2006
$3.5M
NIGMS NIH HHS R01 GM044589NIGMS NIH HHS R01GM44589NIGMS NIH HHS R37 GM047434NIGMS NIH HHS R37GM047434
6 · The paper itself

Abstract

Dynactin is a highly conserved, multiprotein complex that works in conjunction with microtubule-based motors to power a variety of intracellular motile events. Dynamitin (p50) is a core element of dynactin structure. In the present study, we use targeted mutagenesis to evaluate how dynamitin's different structural domains contribute to its ability to self-associate, interact with dynactin and assemble into a complex with its close binding partner, p24. We show that these interactions involve three distinct structural elements: (i) a previously unidentified dimerization motif in the N-terminal 100 amino acids, (ii) an alpha-helical motif spanning aa 106-162 and (iii) the C-terminal half of the molecule (aa 213-406), which is predicted to fold into an antiparallel alpha-helix bundle. The N-terminal half of dynamitin by itself is sufficient to disrupt dynactin, although very high concentrations are required. The ability of mutations in dynamitin's interaction domains to disrupt dynactin in vitro was found to correlate with their inhibitory effects when expressed in cells. We determined that the dynactin subunit, p24, governs dynamitin oligomerization by binding dynamitin along its length. This suppresses aberrant multimerization and drives formation of a protein complex that is identical to the native dynactin shoulder.

Indexed as

MutagenesisProtein ConformationAnimalsCattleChickensDynactin ComplexHumansMicrotubule-Associated ProteinsProtein SubunitsDCTN2 protein, humanDynactin ComplexMicrotubule-Associated ProteinsProtein Subunits

Identifiers

PMID18182012
PMCPMC4157825
OpenAlexW2042662771

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.