Evidence map›Paper›PMID 8991093›Full record

ArticleThe Journal of cell biology1996

Centractin (ARP1) associates with spectrin revealing a potential mechanism to link dynactin to intracellular organelles.

E A Holleran, M K Tokito, S Karki, E L Holzbaur

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of cell biology, 1996. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 85 papers.

0numbers the graph read from it
0cells of the map it votes in
85citing papers in PubMed
13.9field-weighted citation impact, top 1% 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

85 citing papers in PubMed, 225 citations in OpenAlex.

  1. Article
  2. Article
  3. A dual role for βII-spectrin in axons.Proceedings of the National Academy of Sciences of the United States of America · 2019
    Article
  4. Article
  5. Article
  6. The cytoplasmic dynein transport machinery and its many cargoes.Nature reviews. Molecular cell biology · 2018
    Review
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Review
  14. Article
  15. Review
  16. Ordered recruitment of dynactin to the microtubule plus-end is required for efficient initiation of retrograde axonal transport.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2013
    Article
  17. Article
  18. Article
  19. Article
  20. Article

25 more citing papers are in PubMed but not listed here.

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 at 1 institution in 1 country.

E A HolleranCell and Molecular Biology Graduate Group, University of Pennsylvania, Philadelphia 19104, USA.
M K Tokito
S Karki
E L Holzbaur
Philadelphia University · US

Funding

The Interaction of Cytoplasmic Dynein and DynactinR01GM048661 · NIGMS · UNIVERSITY OF PENNSYLVANIA · PI HOLZBAUR, ERIKA L · 1993 to 2017
$6.0M
NIGMS NIH HHS GM48661
6 · The paper itself

Abstract

Centractin (Arp1), an actin-related protein, is a component of the dynactin complex. To investigate potential functions of the protein, we used transient transfections to overexpress centractin in mammalian cells. We observed that the overexpressed polypeptide formed filamentous structures that were significantly longer and more variable in length than those observed in the native dynactin complex. The centractin filaments were distinct from conventional actin in subunit composition and pharmacology as demonstrated by the absence of immunoreactivity of these filaments with an actin-specific antibody, by resistance to treatment with the drug cytochalasin D, and by the inability to bind phalloidin. We examined the transfected cells for evidence of specific associations of the novel centractin filaments with cellular organelles or cytoskeletal proteins. Using immunocytochemistry we observed the colocalization of Golgi marker proteins with the centractin polymers. Additional immunocytochemical analysis using antibodies to non-erythroid spectrin (fodrin) and Golgi-spectrin (beta I sigma *) revealed that spectrin colocalized with the centractin filaments in transfected cells. Biochemical assays demonstrated that spectrin was present in dynactin-enriched cellular fractions, was coimmunoprecipitated from rat brain cytosol using antibodies to dynactin subunits, and was coeluted with dynactin using affinity chromatography. Immunoprecipitations and affinity chromatography also revealed that actin is not a bona fide component of dynactin. Our results indicate that spectrin is associated with the dynactin complex. We suggest a model in which dynactin associates with the Golgi through an interaction between the centractin filament of the dynactin complex and a spectrin-linked cytoskeletal network.

Indexed as

Microtubule-Associated ProteinsActin CytoskeletonActinsAnimalsBiological TransportBiomarkersCell LineChromatography, AffinityCytoskeletonDynactin ComplexGene ExpressionGolgi ApparatusMacropodidaeMicrotubule ProteinsMicrotubulesMolecular Sequence DataActinsBiomarkerscentractinDynactin ComplexMicrotubule-Associated ProteinsMicrotubule ProteinsPolymersSpectrin

Identifiers

PMID8991093
PMCPMC2133946
OpenAlexW2009785604

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
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.