Evidence map›Paper›PMID 34161133›Full record

ArticleMolecular biology of the cell2021

Quantitative live-cell PALM reveals nanoscopic Faa4 redistributions and dynamics on lipid droplets during metabolic transitions of yeast.

Santosh Adhikari, Joe Moscatelli, Elias M Puchner

Open access · greenAbstract read
In one paragraph

Article in Molecular biology of the cell, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.

0numbers the graph read from it
0cells of the map it votes in
8citing papers in PubMed
1.2field-weighted citation impact, top 23% 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

8 citing papers in PubMed, 10 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

3 authors at 1 institution in 1 country.

Santosh AdhikariSchool of Physics and Astronomy, University of Minnesota, Twin Cities, Physics and Nanotechnology (PAN), Minneapolis, MN 55455.
Joe MoscatelliSchool of Physics and Astronomy, University of Minnesota, Twin Cities, Physics and Nanotechnology (PAN), Minneapolis, MN 55455.
Elias M PuchnerSchool of Physics and Astronomy, University of Minnesota, Twin Cities, Physics and Nanotechnology (PAN), Minneapolis, MN 55455.
University of Minnesota · US

Funding

Developing Diffusion-Contrast Super-Resolution Microscopy to Study Protein Interactions at Extreme Concentration Ratios in Live CellsR21GM127965 · NIGMS · UNIVERSITY OF MINNESOTA · PI PUCHNER, GEORG ELIAS MICHAEL · 2018 to 2019
$283k
NIGMS NIH HHS R21 GM127965
6 · The paper itself

Abstract

Lipid droplets (LDs) are dynamic organelles for lipid storage and homeostasis. Cells respond to metabolic changes by regulating the spatial distribution of LDs and enzymes required for LD growth and turnover. The small size of LDs precludes the observation of their associated enzyme densities and dynamics with conventional fluorescence microscopy. Here we employ quantitative photo-activated localization microscopy to study the density of the fatty acid (FA) activating enzyme Faa4 on LDs in live yeast cells with single-molecule sensitivity and 30 nm resolution. During the log phase LDs colocalize with the endoplasmic reticulum (ER) where their emergence and expansion are mediated by the highest observed Faa4 densities. During transition to the stationary phase, LDs with a ∼2-fold increased surface area translocate to the vacuolar surface and lumen and exhibit a ∼2.5-fold increase in Faa4 density. The increased Faa4 density on LDs further suggests its role in LD expansion, is caused by its ∼5-fold increased expression level, and is specific to exogenous FA chain-lengths. When lipolysis is induced by refreshed medium, Faa4 shuttles through ER- and lipophagy to the vacuole, where it may activate FAs for membrane expansion and degrade Faa4 to reset its cellular abundance to levels in the log phase.

Indexed as

Acyl Coenzyme AAutophagyEndoplasmic ReticulumFatty AcidsHomeostasisLipid DropletsLipid MetabolismLipolysisSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsVacuolesAcyl Coenzyme AFAA4 protein, S cerevisiaeFatty AcidsSaccharomyces cerevisiae Proteins

Identifiers

PMID34161133
PMCPMC8351750
OpenAlexW3176483927

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
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.