Evidence map›Paper›PMID 37619984›Full record

ArticlePlant physiology2023

CALEOSIN 1 interaction with AUTOPHAGY-RELATED PROTEIN 8 facilitates lipid droplet microautophagy in seedlings.

Magdalena Miklaszewska, Krzysztof Zienkiewicz, Ewa Klugier-Borowska, Marcin Rygielski, Ivo Feussner, Agnieszka Zienkiewicz

Open access · hybridAbstract read
In one paragraph

Article in Plant physiology, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
5.3field-weighted citation impact, top 4% 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

19 citing papers in PubMed, 30 citations in OpenAlex.

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  5. Characterization ofPlants (Basel, Switzerland) · 2025
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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

6 authors at 3 institutions in 2 countries.

Magdalena MiklaszewskaDepartment of Plant Physiology and Biotechnology, University of Gdańsk, Wita Stwosza 59, Gdańsk 80-308, Poland.ORCID 0000-0002-7108-4761
Krzysztof ZienkiewiczDepartment for Plant Biochemistry, Albrecht-von-Haller-Institute for Plant Sciences, University of Goettingen, Justus-von-Liebig-Weg 11, Goettingen 37077, Germany.ORCID 0000-0002-8525-9569
Ewa Klugier-BorowskaCentre for Modern Interdisciplinary Technologies, Nicolaus Copernicus University in Toruń, Wileńska 4, 87-100 Toruń, Poland.
Marcin RygielskiCentre for Modern Interdisciplinary Technologies, Nicolaus Copernicus University in Toruń, Wileńska 4, 87-100 Toruń, Poland.ORCID 0000-0001-5126-5947
Ivo FeussnerDepartment for Plant Biochemistry, Albrecht-von-Haller-Institute for Plant Sciences, University of Goettingen, Justus-von-Liebig-Weg 11, Goettingen 37077, Germany.ORCID 0000-0002-9888-7003
Agnieszka ZienkiewiczDepartment for Plant Biochemistry, Albrecht-von-Haller-Institute for Plant Sciences, University of Goettingen, Justus-von-Liebig-Weg 11, Goettingen 37077, Germany.ORCID 0000-0003-0799-0521
Nicolaus Copernicus University · PLUniversity of Gdańsk · PLUniversity of Göttingen · DE

Funding

Polish Ministry of Science and Higher Education 1643/MOB/V/2017/0Polish National Science Centre UMO-2019/34/E/NZ1/00023
6 · The paper itself

Abstract

Lipid droplets (LDs) of seed tissues are storage organelles for triacylglycerols (TAGs) that provide the energy and carbon for seedling establishment. In the major route of LD degradation (lipolysis), TAGs are mobilized by lipases. However, LDs may also be degraded via lipophagy, a type of selective autophagy, which mediates LD delivery to vacuoles or lysosomes. The exact mechanisms of LD degradation and the mobilization of their content in plants remain unresolved. Here, we provide evidence that LDs are degraded via a process morphologically resembling microlipophagy in Arabidopsis (Arabidopsis thaliana) seedlings. We observed the entry and presence of LDs in the central vacuole as well as their breakdown. Moreover, we show co-localization of AUTOPHAGY-RELATED PROTEIN 8b (ATG8b) and LDs during seed germination and localization of lipidated ATG8 (ATG8-PE) to the LD fraction. We further demonstrate that structural LD proteins from the caleosin family, CALEOSIN 1 (CLO1), CALEOSIN 2 (CLO2), and CALEOSIN 3 (CLO3), interact with ATG8 proteins and possess putative ATG8-interacting motifs (AIMs). Deletion of the AIM localized directly before the proline knot disrupts the interaction of CLO1 with ATG8b, suggesting a possible role of this region in the interaction between these proteins. Collectively, we provide insights into LD degradation by microlipophagy in germinating seeds with a particular focus on the role of structural LD proteins in this process.

Indexed as

ArabidopsisSeedlingsArabidopsis ProteinsAutophagyAutophagy-Related Protein 8 FamilyAutophagy-Related ProteinsCalcium-Binding ProteinsLipid DropletsMicroautophagyMixed Function OxygenasesPlant ProteinsTriglyceridesArabidopsis ProteinsATG8 protein, ArabidopsisAutophagy-Related Protein 8 FamilyAutophagy-Related ProteinsCalcium-Binding Proteinscaleosin protein, Sesamum indicumMixed Function OxygenasesperoxygenasePlant ProteinsTriglycerides

Identifiers

PMID37619984
PMCPMC10663143
OpenAlexW4386127303

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.