Evidence map›Paper›PMID 30120248›Full record

ArticleNature communications2018

Insights into degradation mechanism of N-end rule substrates by p62/SQSTM1 autophagy adapter.

Do Hoon Kwon, Ok Hyun Park, Leehyeon Kim, Yang Ouk Jung, Yeonkyoung Park, Hyeongseop Jeong, Jaekyung Hyun, Yoon Ki Kim, Hyun Kyu Song

Abstract read
In one paragraph

Article in Nature communications, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 55 papers, 2 of them syntheses that pooled it.

0numbers the graph read from it
0cells of the map it votes in
55citing papers in PubMed, 2 pooled it
–field-weighted citation impact
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

55 citing papers in PubMed, 2 syntheses or guidelines pooled it.

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4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

9 authors.

Do Hoon KwonDepartment of Life Sciences, Korea University, Seoul, 02841, Korea.ORCID http://orcid.org/0000-0002-3214-3394
Ok Hyun ParkDepartment of Life Sciences, Korea University, Seoul, 02841, Korea.
Leehyeon KimDepartment of Life Sciences, Korea University, Seoul, 02841, Korea.ORCID http://orcid.org/0000-0002-1266-7828
Yang Ouk JungDepartment of Life Sciences, Korea University, Seoul, 02841, Korea.ORCID http://orcid.org/0000-0001-6410-4165
Yeonkyoung ParkDepartment of Life Sciences, Korea University, Seoul, 02841, Korea.
Hyeongseop JeongElectron Microscopy Research Center, Korea Basic Science Institute, Chungcheongbuk-do, 28119, Korea.
Jaekyung HyunElectron Microscopy Research Center, Korea Basic Science Institute, Chungcheongbuk-do, 28119, Korea.
Yoon Ki KimDepartment of Life Sciences, Korea University, Seoul, 02841, Korea.ORCID http://orcid.org/0000-0003-1303-072X
Hyun Kyu SongDepartment of Life Sciences, Korea University, Seoul, 02841, Korea. hksong@korea.ac.kr.ORCID http://orcid.org/0000-0001-5684-4059

Funding

National Research Foundation of Korea (NRF) BRL grant: No. 2015041919National Research Foundation of Korea (NRF) International Cooperation Program: No. 2015K2A2A6002008National Research Foundation of Korea (NRF) NRF-2016R1E1A1A01942623
6 · The paper itself

Abstract

p62/SQSTM1 is the key autophagy adapter protein and the hub of multi-cellular signaling. It was recently reported that autophagy and N-end rule pathways are linked via p62. However, the exact recognition mode of degrading substrates and regulation of p62 in the autophagic pathway remain unknown. Here, we present the complex structures between the ZZ-domain of p62 and various type-1 and type-2 N-degrons. The binding mode employed in the interaction of the ZZ-domain with N-degrons differs from that employed by classic N-recognins. It was also determined that oligomerization via the PB1 domain can control functional affinity to the R-BiP substrate. Unexpectedly, we found that self-oligomerization and disassembly of p62 are pH-dependent. These findings broaden our understanding of the functional repertoire of the N-end rule pathway and provide an insight into the regulation of p62 during the autophagic pathway.

Indexed as

AutophagyProteolysisAmino Acid SequenceEndoplasmic Reticulum Chaperone BiPHeat-Shock ProteinsHeLa CellsHumansHydrogen-Ion ConcentrationModels, BiologicalModels, MolecularMutationProtein AggregatesProtein BindingProtein DomainsProtein MultimerizationSequestosome-1 ProteinEndoplasmic Reticulum Chaperone BiPHeat-Shock ProteinsProtein AggregatesSequestosome-1 Protein

Identifiers

PMID30120248
PMCPMC6098011

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Registered trials

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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.