Evidence map›Paper›PMID 8978670›Full record

ArticleThe EMBO journal1996

Fission yeast Sop2p: a novel and evolutionarily conserved protein that interacts with Arp3p and modulates profilin function.

M K Balasubramanian, A Feoktistova, D McCollum, K L Gould

Open access · greenAbstract readComparative Study
In one paragraph

Article in The EMBO journal, 1996. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 50 papers.

0numbers the graph read from it
0cells of the map it votes in
50citing papers in PubMed
4.0field-weighted citation impact, top 5% 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

50 citing papers in PubMed, 88 citations in OpenAlex.

  1. Article
  2. Effects ofExperimental and therapeutic medicine · 2026
    Article
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  4. Article
  5. Article
  6. Article
  7. The Tbx6 Transcription Factor Dorsocross Mediates Dpp Signaling to RegulateInternational journal of molecular sciences · 2022
    Article
  8. Article
  9. Review
  10. Article
  11. Article
  12. The Diverse Family of Arp2/3 Complexes.Trends in cell biology · 2017
    Review
  13. Article
  14. Article
  15. Article
  16. Article
  17. Actin cytoskeleton: a nucleator face-off.Current biology : CB · 2014
    Article
  18. Article
  19. Article
  20. 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

4 authors at 1 institution in 1 country.

M K BalasubramanianHoward Hughes Medical Institute and Department of Cell Biology, Vanderbilt University School of Medicine, Nashville, TN 37232, USA.
A Feoktistova
D McCollum
K L Gould
Howard Hughes Medical Institute · US

Funding

MITOTIC CONTROL GENE CDC28F32GM016145 · NIGMS · VANDERBILT UNIVERSITY · PI MCCOLLUM, DANNEL · 1993 to 1995
–
NIGMS NIH HHS GM16145
6 · The paper itself

Abstract

Profilins bind to monomeric actin and also interact with ligands such as phosphoinositide 4,5-bisphosphate, the proline-rich protein VASP and a complex of four to six polypeptides identified in Acanthamoeba that includes two actin-related proteins. Here, we report the identification and characterization of an essential gene from Schizosaccharomyces pombe, sop2+, a mutation in which rescues the temperature-sensitive lethality of a profilin mutation, cdc3-124. The sop2-1 mutant is defective for cell elongation and septation, suggesting that it is involved in multiple cortical actin-requiring processes. Consistent with a role in actin cytoskeletal function, negative interactions have been identified between sop2-1 and act1-48, a mutant allele of actin. Sop2p is a novel 377 amino acid polypeptide with similarity to proteins of the beta-transducin repeat family. Sop2p-related proteins have been identified by sequencing projects in diverse species, and we have isolated a human cDNA highly related to sop2+, SOP2 Hs, which functionally complements the sop2-1 mutation. Sop2p proteins from all species contain peptide sequences identical or highly similar to two peptide sequences from an Acanthamoeba beta-transducin repeat protein present in the profilin binding complex. Biochemical analyses demonstrate that Sop2p is present in a complex which also contains the actin-related protein, Arp3p. Immunofluorescence studies reveal the presence of Sop2p in (i) punctate structures distributed throughout the cell, (ii) cables that extend the length of the cell, and (iii) a medial band in a small percentage of septating cells. Collectively these data demonstrate the interaction of Sop2p with Arp3p, profilin and actin.

Indexed as

Contractile ProteinsGenes, FungalSchizosaccharomyces pombe ProteinsAcanthamoebaActinsAmino Acid SequenceAnimalsBase SequenceCarrier ProteinsConserved SequenceCytoskeletal ProteinsDNA, ComplementaryDrosophilaGenotypeHumansMicrofilament ProteinsActinsarc1 protein, S pombeCarrier ProteinsContractile ProteinsCytoskeletal ProteinsDNA, ComplementaryMicrofilament ProteinsProfilinsSchizosaccharomyces pombe Proteins

Identifiers

PMID8978670
PMCPMC452468
OpenAlexW2419450110

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.