Evidence map›Paper›PMID 25138357›Full record

ReviewIUBMB life2014

Yeast studies reveal moonlighting functions of the ancient actin cytoskeleton.

Evelyn Sattlegger, Tatiana A Chernova, Neeku M Gogoi, Indu V Pillai, Yury O Chernoff, Alan L Munn

Open access · bronzeAbstract readReview
In one paragraph

Review in IUBMB life, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.

0numbers the graph read from it
0cells of the map it votes in
9citing papers in PubMed
0.8field-weighted citation impact, top 32% 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

9 citing papers in PubMed, 15 citations in OpenAlex.

  1. Article
  2. A census of actin-associated proteins in humans.Frontiers in cell and developmental biology · 2023
    Article
  3. Review
  4. Article
  5. Article
  6. Review
  7. Article
  8. Article
  9. 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 5 institutions in 5 countries.

Evelyn SattleggerInstitute of Natural and Mathematical Sciences, Massey University, Albany, New Zealand.
Tatiana A Chernova
Neeku M Gogoi
Indu V Pillai
Yury O Chernoff
Alan L Munn
Amity University · INEmory University · USGriffith University · AUMassey University · NZSt Petersburg University · RU

Funding

Ubiquitin and regulation of prion induction by a short-lived proteinR01GM093294 · NIGMS · EMORY UNIVERSITY · PI WILKINSON, KEITH D · 2011 to 2014
$1.3M
NIGMS NIH HHS R01 GM093294NIGMS NIH HHS R01GM093294
6 · The paper itself

Abstract

Classic functions of the actin cytoskeleton include control of cell size and shape and the internal organization of cells. These functions are manifest in cellular processes of fundamental importance throughout biology such as the generation of cell polarity, cell migration, cell adhesion, and cell division. However, studies in the unicellular model eukaryote Saccharomyces cerevisiae (Baker's yeast) are giving insights into other functions in which the actin cytoskeleton plays a critical role. These include endocytosis, control of protein translation, and determination of protein 3-dimensional shape (especially conversion of normal cellular proteins into prions). Here, we present a concise overview of these new "moonlighting" roles for the actin cytoskeleton and how some of these roles might lie at the heart of important molecular switches. This is an exciting time for researchers interested in the actin cytoskeleton. We show here how studies of actin are leading us into many new and exciting realms at the interface of genetics, biochemistry, and cell biology. While many of the pioneering studies have been conducted using yeast, the conservation of the actin cytoskeleton and its component proteins throughout eukaryotes suggests that these new roles for the actin cytoskeleton may not be restricted to yeast cells but rather may reflect new roles for the actin cytoskeleton of all eukaryotes.

Indexed as

Biological EvolutionProtein ConformationActin CytoskeletonCytoskeletal ProteinsEndocytosisModels, BiologicalProtein BiosynthesisProtein FoldingSaccharomyces cerevisiaeSpecies SpecificityCytoskeletal ProteinsamyloidArp2/3eEF1AforminLsb2pSup35pYih1p

Identifiers

PMID25138357
PMCPMC4176509
OpenAlexW1604910734

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.