Evidence map›Paper›PMID 18400761›Full record

ArticleThe Journal of biological chemistry2008

Interactions between the yeast SM22 homologue Scp1 and actin demonstrate the importance of actin bundling in endocytosis.

Dana M Gheorghe, Soheil Aghamohammadzadeh, Iwona I Smaczynska-de Rooij, Ellen G Allwood, Steve J Winder, Kathryn R Ayscough

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.

0numbers the graph read from it
0cells of the map it votes in
32citing papers in PubMed
2.0field-weighted citation impact, top 15% 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

32 citing papers in PubMed, 42 citations in OpenAlex.

  1. A role for cross-linking proteins in actin filament network organization and force generation.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  2. Article
  3. Review
  4. Article
  5. Article
  6. Plastin 3 in health and disease: a matter of balance.Cellular and molecular life sciences : CMLS · 2021
    Review
  7. Article
  8. Article
  9. TwoThe Journal of biological chemistry · 2020
    Article
  10. Article
  11. Article
  12. The Impact of ESCRT on AβFrontiers in molecular neuroscience · 2018
    Article
  13. Article
  14. Article
  15. Review
  16. Article
  17. 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

6 authors at 1 institution in 1 country.

Dana M GheorgheDepartments of Molecular Biology and Biotechnology, Biomedical Science, University of Sheffield, Sheffield, S10 2TN, United Kingdom.
Soheil Aghamohammadzadeh
Iwona I Smaczynska-de Rooij
Ellen G Allwood
Steve J Winder
Kathryn R Ayscough
University of Sheffield · GB

Funding

Biotechnology and Biological Sciences Research Council BB/C510091/1Medical Research Council G117/394Medical Research Council G117/394(66695)Wellcome Trust 07479/Z/04/ZWellcome Trust 074979Wellcome Trust GR077544AIA
6 · The paper itself

Abstract

The yeast SM22 homologue Scp1 has previously been shown to act as an actin-bundling protein in vitro. In cells, Scp1 localizes to the cortical actin patches that form as part of the invagination process during endocytosis, and its function overlaps with that of the well characterized yeast fimbrin homologue Sac6p. In this work we have used live cell imaging to demonstrate the importance of key residues in the Scp1 actin interface. We have defined two actin binding domains within Scp1 that allow the protein to both bind and bundle actin without the need for dimerization. Green fluorescent protein-tagged mutants of Scp1 also indicate that actin localization does not require the putative phosphorylation site Ser-185 to be functional. Deletion of SCP1 has few discernable effects on cell growth and morphology. However, we reveal that scp1 deletion is compensated for by up-regulation of Sac6. Furthermore, Scp1 levels are increased in the absence of sac6. The presence of compensatory pathways to up-regulate Sac6 or Scp1 levels in the absence of the other suggest that maintenance of sufficient bundling activity is critical within the cell. Analysis of cortical patch assembly and movement during endocytosis reveals a previously undetected role for Scp1 in movement of patches away from the plasma membrane. Additionally, we observe a dramatic increase in patch lifetime in a strain lacking both sac6 and scp1, demonstrating the central role played by actin-bundling proteins in the endocytic process.

Indexed as

ActinsDimerizationEndocytosisMembrane GlycoproteinsMicrofilament ProteinsPhosphorylationProtein BindingProtein Structure, TertiarySaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsActinsMembrane GlycoproteinsMicrofilament ProteinsplastinSaccharomyces cerevisiae ProteinsSCP1 protein, S cerevisiae

Identifiers

PMID18400761
PMCPMC2397485
OpenAlexW2082485257

What OpenQuestion holds

Textmetadata
LicenceTDM
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.