Evidence map›Paper›PMID 16231104›Full record

ReviewProtoplasma2005

Coupling actin dynamics to the endocytic process in Saccharomyces cerevisiae.

K R Ayscough

Abstract readReview
PubMed Publisher
In one paragraph

Review in Protoplasma, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
1.5field-weighted citation impact, top 20% 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

13 citing papers in PubMed, 28 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Article
  5. Article
  6. Article
  7. pH-dependent cargo sorting from the Golgi.The Journal of biological chemistry · 2011
    Article
  8. Actin and endocytosis: mechanisms and phylogeny.Current opinion in cell biology · 2009
    Review
  9. Article
  10. Auxin transport inhibitors impair vesicle motility and actin cytoskeleton dynamics in diverse eukaryotes.Proceedings of the National Academy of Sciences of the United States of America · 2008
    Article
  11. Article
  12. Review
  13. 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

1 author at 1 institution in 1 country.

K R AyscoughDepartment of Molecular Biology and Biotechnology, University of Sheffield, Sheffield, United Kingdom.
University of Sheffield · GB

Funding

Medical Research Council G117/394
6 · The paper itself

Abstract

Endocytosis is an essential eukaryotic process that, in many systems, has been reported to require a functional actin cytoskeleton. The process of endocytosis is critical for controlling the protein-lipid composition of the plasma membrane and uptake of nutrients as well as pathogens and also plays an important role in regulation of cell signalling. While several distinct pathways for endocytosis have been characterised, all of these require remodelling of the cell cortex. The importance of a dynamic actin cytoskeleton for facilitating endocytosis has been recognised for many years in budding yeast and is increasingly supported by studies in mammalian cells. Current evidence suggests that cortical patches are sites of endocytosis in Saccharomyces cerevisiae and that these sites are composed of sequentially forming protein complexes. Distinct stages in complex formation are characterised by the presence of different activators of F-actin polymerisation. Disassembly of the complexes is also essential for the endocytosis to proceed. Mutants lacking the kinases Ark1 and Prk1 accumulate actin and endocytic machinery in a single large clump in cells. Phosphorylation of endocytic proteins including Sla1p is proposed to cause their removal from the complex and allow later stages of the invagination process to occur. Dephosphorylation of endocytic components may then allow subsequent reincorporation into new sites of endocytic complex assembly.

Indexed as

ActinsBridged Bicyclo Compounds, HeterocyclicCarrier ProteinsCytoskeletal ProteinsEndocytosisMicroscopy, FluorescenceModels, MolecularMutationPhosphorylationProtein Kinase CSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsThiazolesThiazolidinesActinsBridged Bicyclo Compounds, HeterocyclicCarrier ProteinsCytoskeletal Proteinslatrunculin AProtein Kinase Cprotein kinase NSaccharomyces cerevisiae ProteinsSLA1 protein, S cerevisiaeThiazolesThiazolidines

Identifiers

PMID16231104
OpenAlexW2161330661

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.