Evidence map›Paper›PMID 25484070›Full record

ReviewAutophagy2015

Posttranslational modification of autophagy-related proteins in macroautophagy.

Yangchun Xie, Rui Kang, Xiaofang Sun, Meizuo Zhong, Jin Huang, Daniel J Klionsky, Daolin Tang

Open access · bronzeAbstract readReview
In one paragraph

Review in Autophagy, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 215 papers, 3 of them syntheses that pooled it.

0numbers the graph read from it
0cells of the map it votes in
215citing papers in PubMed, 3 pooled it
11.2field-weighted citation impact, top 1% 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

215 citing papers in PubMed, 3 syntheses or guidelines pooled it, 309 citations in OpenAlex.

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155 more citing papers are in PubMed but not listed here.

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

7 authors at 5 institutions in 2 countries.

Yangchun Xiea Department of Oncology; Xiangya Hospital ; Central South University ; Changsha , Hunan , China.
Rui Kang
Xiaofang Sun
Meizuo Zhong
Jin Huang
Daniel J Klionsky
Daolin Tang
Central South University · CNUniversity of Pittsburgh · USKey Laboratory of Guangdong Province · CNUniversity of Michigan–Ann Arbor · USUPMC Hillman Cancer Center · US

Funding

VECTOR CORE FACILITYP30CA047904 · NCI · UNIVERSITY OF PITTSBURGH AT PITTSBURGH · PI Leonard J. Appleman · 1988 to 2026
$158.0M
ALTERNATIVE VACUOLAR TARGETING MECHANISMS IN YEASTR01GM053396 · NIGMS · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI KLIONSKY, DANIEL J. · 1995 to 2018
$12.1M
Targeting HMGB1-mediated Autophagy in Cancer TherapyR01CA160417 · NCI · UT SOUTHWESTERN MEDICAL CENTER · PI TANG, DAOLIN · 2012 to 2023
$3.0M
NCI NIH HHS P30CA047904NCI NIH HHS R01CA160417NIGMS NIH HHS R01 GM053396NIGMS NIH HHS R01GM053396
6 · The paper itself

Abstract

Macroautophagy is an intracellular catabolic process involved in the formation of multiple membrane structures ranging from phagophores to autophagosomes and autolysosomes. Dysfunction of macroautophagy is implicated in both physiological and pathological conditions. To date, 38 autophagy-related (ATG) genes have been identified as controlling these complicated membrane dynamics during macroautophagy in yeast; approximately half of these genes are clearly conserved up to human, and there are additional genes whose products function in autophagy in higher eukaryotes that are not found in yeast. The function of the ATG proteins, in particular their ability to interact with a number of macroautophagic regulators, is modulated by posttranslational modifications (PTMs) such as phosphorylation, glycosylation, ubiquitination, acetylation, lipidation, and proteolysis. In this review, we summarize our current knowledge of the role of ATG protein PTMs and their functional relevance in macroautophagy. Unraveling how these PTMs regulate ATG protein function during macroautophagy will not only reveal fundamental mechanistic insights into the regulatory process, but also provide new therapeutic targets for the treatment of autophagy-associated diseases.

Indexed as

AutophagyProtein Processing, Post-TranslationalAnimalsHumansMicrotubule-Associated ProteinsModels, BiologicalMicrotubule-Associated ProteinsAMPK, AMP-activated protein kinaseATG, autophagy-relatedautophagyautophagy-related proteinsMTORC1, mechanistic target of rapamycin complex 1PE, phosphatidylethanolamineposttranslational modificationPTM, posttranslational modificationUbl, ubiquitin likeUb, ubiquitin

Identifiers

PMID25484070
PMCPMC4502723
OpenAlexW2067490363

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.