Evidence map›Paper›PMID 26914139›Full record

ArticleeLife2016

Yeast Eps15-like endocytic protein Pan1p regulates the interaction between endocytic vesicles, endosomes and the actin cytoskeleton.

Junko Y Toshima, Eri Furuya, Makoto Nagano, Chisa Kanno, Yuta Sakamoto, Masashi Ebihara, Daria Elisabeth Siekhaus, Jiro Toshima

Open access · goldAbstract read
In one paragraph

Article in eLife, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
0.9field-weighted citation impact, top 27% 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

12 citing papers in PubMed, 20 citations in OpenAlex.

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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

8 authors at 3 institutions in 2 countries.

Junko Y ToshimaDepartment of Liberal Arts, Tokyo University of Technology, Tokyo, Japan.
Eri FuruyaDepartment of Biological Science and Technology, Tokyo University of Science, Tokyo, Japan.
Makoto NaganoResearch Center for RNA Science, Tokyo University of Science, Tokyo, Japan.
Chisa KannoDepartment of Biological Science and Technology, Tokyo University of Science, Tokyo, Japan.
Yuta SakamotoDepartment of Biological Science and Technology, Tokyo University of Science, Tokyo, Japan.
Masashi EbiharaDepartment of Biological Science and Technology, Tokyo University of Science, Tokyo, Japan.
Daria Elisabeth SiekhausInstitute of Science and Technology Austria, Klosterneuburg, Austria.
Jiro ToshimaResearch Center for RNA Science, Tokyo University of Science, Tokyo, Japan.ORCID http://orcid.org/0000-0003-3264-9843
Tokyo University of Science · JPTokyo University of Technology · JPInstitute of Science and Technology Austria · AT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The actin cytoskeleton plays important roles in the formation and internalization of endocytic vesicles. In yeast, endocytic vesicles move towards early endosomes along actin cables, however, the molecular machinery regulating interaction between endocytic vesicles and actin cables is poorly understood. The Eps15-like protein Pan1p plays a key role in actin-mediated endocytosis and is negatively regulated by Ark1 and Prk1 kinases. Here we show that pan1 mutated to prevent phosphorylation at all 18 threonines, pan1-18TA, displayed almost the same endocytic defect as ark1Δ prk1Δ cells, and contained abnormal actin concentrations including several endocytic compartments. Early endosomes were highly localized in the actin concentrations and displayed movement along actin cables. The dephosphorylated form of Pan1p also caused stable associations between endocytic vesicles and actin cables, and between endocytic vesicles and endosomes. Thus Pan1 phosphorylation is part of a novel mechanism that regulates endocytic compartment interactions with each other and with actin cables.

Indexed as

Actin CytoskeletonAmino Acid SubstitutionDNA Mutational AnalysisEndosomesMicrofilament ProteinsMutagenesis, Site-DirectedPhosphorylationProtein Processing, Post-TranslationalSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsTransport VesiclesMicrofilament ProteinsPAN1 protein, S cerevisiaeSaccharomyces cerevisiae Proteinsactincell biologyclathrinendocytosisendosome<i>s. cerevisiae</i>

Identifiers

PMID26914139
PMCPMC4775215
OpenAlexW2276424698

What OpenQuestion holds

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LicenceCC BY
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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.