Evidence map›Paper›PMID 27325703›Full record

ArticleThe Journal of biological chemistry2016

RACK1 Is an Interaction Partner of ATG5 and a Novel Regulator of Autophagy.

Secil Erbil, Ozlem Oral, Geraldine Mitou, Cenk Kig, Emel Durmaz-Timucin, Emine Guven-Maiorov, Ferah Gulacti, Gokcen Gokce, Jörn Dengjel, Osman Ugur Sezerman and 1 more

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed
3.6field-weighted citation impact, top 7% 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

25 citing papers in PubMed, 55 citations in OpenAlex.

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  15. Crosstalk between autophagy and DNA repair systems.Turkish journal of biology = Turk biyoloji dergisi · 2021
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  18. Chlorogenic Acid Alleviates AβDrug design, development and therapy · 2020
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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

11 authors at 4 institutions in 2 countries.

Secil ErbilFrom the Molecular Biology, Genetics and Bioengineering Program, Sabanci University, Orhanli-Tuzla, 34956 Istanbul, Turkey.
Ozlem OralFrom the Molecular Biology, Genetics and Bioengineering Program, Sabanci University, Orhanli-Tuzla, 34956 Istanbul, Turkey.
Geraldine MitouFrom the Molecular Biology, Genetics and Bioengineering Program, Sabanci University, Orhanli-Tuzla, 34956 Istanbul, Turkey.
Cenk KigFrom the Molecular Biology, Genetics and Bioengineering Program, Sabanci University, Orhanli-Tuzla, 34956 Istanbul, Turkey.
Emel Durmaz-TimucinFrom the Molecular Biology, Genetics and Bioengineering Program, Sabanci University, Orhanli-Tuzla, 34956 Istanbul, Turkey.
Emine Guven-Maiorovthe Department of Chemical and Biological Engineering and Center for Computational Biology and Bioinformatics, Koc University, 34450 Istanbul, Turkey.
Ferah GulactiFrom the Molecular Biology, Genetics and Bioengineering Program, Sabanci University, Orhanli-Tuzla, 34956 Istanbul, Turkey.
Gokcen GokceFrom the Molecular Biology, Genetics and Bioengineering Program, Sabanci University, Orhanli-Tuzla, 34956 Istanbul, Turkey.
Jörn Dengjelthe Department of Biology, University of Fribourg, Chemin du Musée 10, CH-1700 Fribourg, Switzerland, and.
Osman Ugur Sezermanthe Department of Biostatistics and Medical Informatics, School of Medicine, Acibadem University, Atasehir, 34752 İstanbul, Turkey.
Devrim GozuacikFrom the Molecular Biology, Genetics and Bioengineering Program, Sabanci University, Orhanli-Tuzla, 34956 Istanbul, Turkey, dgozuacik@sabanciuniv.edu.
Sabancı Üniversitesi · TRAcıbadem University · TRKoç University · TRUniversity of Fribourg · CH

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Autophagy is biological mechanism allowing recycling of long-lived proteins, abnormal protein aggregates, and damaged organelles under cellular stress conditions. Following sequestration in double- or multimembrane autophagic vesicles, the cargo is delivered to lysosomes for degradation. ATG5 is a key component of an E3-like ATG12-ATG5-ATG16 protein complex that catalyzes conjugation of the MAP1LC3 protein to lipids, thus controlling autophagic vesicle formation and expansion. Accumulating data indicate that ATG5 is a convergence point for autophagy regulation. Here, we describe the scaffold protein RACK1 (receptor activated C-kinase 1, GNB2L1) as a novel ATG5 interactor and an autophagy protein. Using several independent techniques, we showed that RACK1 interacted with ATG5. Importantly, classical autophagy inducers (starvation or mammalian target of rapamycin blockage) stimulated RACK1-ATG5 interaction. Knockdown of RACK1 or prevention of its binding to ATG5 using mutagenesis blocked autophagy activation. Therefore, the scaffold protein RACK1 is a new ATG5-interacting protein and an important and novel component of the autophagy pathways.

Indexed as

AnimalsAutophagyAutophagy-Related Protein 12Autophagy-Related Protein 5Autophagy-Related ProteinsGTP-Binding ProteinsHEK293 CellsHumansMiceNeoplasm ProteinsProtein BindingReceptors, Cell SurfaceReceptors for Activated C KinaseATG12 protein, humanATG16L1 protein, humanATG5 protein, humanAutophagy-Related Protein 12Autophagy-Related Protein 5Autophagy-Related ProteinsGTP-Binding ProteinsNeoplasm ProteinsRACK1 protein, humanReceptors, Cell SurfaceReceptors for Activated C KinaseATG12-5-16ATG5autophagylysosomemammalian target of rapamycin (mTOR)p70S6Kprotein-protein interactionRACK1signaling

Identifiers

PMID27325703
PMCPMC4974388
OpenAlexW2468305494

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.