Evidence map›Paper›PMID 36042481›Full record

ArticleCell communication and signaling : CCS2022

GNIP1 functions both as a scaffold protein and an E3 ubiquitin ligase to regulate autophagy in lung cancer.

Feifei Zhou, Yufeng Liu, Wenqian Ai, Yanan Wang, Mingxi Gan, Qingkun Jiang, Tianyu Han, Jian-Bin Wang

Open access · goldAbstract readVideo-Audio Media
In one paragraph

Article in Cell communication and signaling : CCS, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing papers in PubMed
0.5field-weighted citation impact, top 38% 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

2 citing papers in PubMed, 6 citations in OpenAlex.

  1. Review
  2. Advances of E3 ligases in lung cancer.Biochemistry and biophysics reports · 2024
    Review
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

8 authors at 2 institutions in 1 country.

Feifei ZhouSchool of Basic Medical Sciences, Nanchang University, Nanchang, 330031, People's Republic of China.
Yufeng LiuSchool of Basic Medical Sciences, Nanchang University, Nanchang, 330031, People's Republic of China.
Wenqian AiSchool of Basic Medical Sciences, Nanchang University, Nanchang, 330031, People's Republic of China.
Yanan WangJiangxi Institute of Respiratory Disease, The First Affiliated Hospital of Nanchang University, Nanchang, 330006, People's Republic of China.
Mingxi GanSchool of Basic Medical Sciences, Nanchang University, Nanchang, 330031, People's Republic of China.
Qingkun JiangDepartment of Oral and Maxillofacial Surgery, First Affiliated Hospital of Nanchang University, Nanchang, 330006, People's Republic of China.
Tianyu HanJiangxi Institute of Respiratory Disease, The First Affiliated Hospital of Nanchang University, Nanchang, 330006, People's Republic of China. hantianyu87@163.com.
Jian-Bin WangSchool of Basic Medical Sciences, Nanchang University, Nanchang, 330031, People's Republic of China. jianbinwang@ncu.edu.cn.
First Affiliated Hospital of Nanchang University · CNNanchang University · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

backgroundGlycogen-Interacting Protein 1 (GNIP1), an E3 ligase, is a member of the tripartite motif (TRIM) family proteins. Current studies on GNIP1 mainly focus on glycogen metabolism. However, the function and molecular mechanisms of GNIP1 in regulating autophagy still remains unclear. This study aimed to investigate the regulatory mechanism of GNIP1 in regulating autophagy in non-small cell lung cancer (NSCLC).

methodsCrystal violet staining assays were used to evaluate the ability of cell growth and proliferation. Transwell and scratch wound healing assays were used to evaluate the cell migration ability. The protein expressions were measured by western blot and immunohistochemistry. Co-immunoprecipitation assays determined the protein-protein interactions. The in vivo effect of GNIP1 on tumor growth was determined by xenograft assay.

resultsWe found that GNIP1 was overexpressed in tumor tissues and the expression level of GNIP1 was related to the poor prognosis and the survival time of NSCLC patients. In non-small cell lung cancer (NSCLC), GNIP1 increased proliferation and migration of cancer cells by promoting autophagy. Mechanistic studies indicated that GNIP1, as a scaffold protein, recruited BECN1 and LC3B to promote the formation of autophagosomes. Besides, GNIP1 mediated the degradation of 14-3-3ζ, the negative regulator of VPS34 complex, thus promoting autophagy. Overexpressing GNIP1 promoted tumorigenesis and enhanced autophagy in xenograft models.

conclusionGNIP1 promotes proliferation and migration of NSCLC cells through mediating autophagy, which provides theoretical basis for targeting GNIP1 as anti-cancer drugs. Video Abstract.

Indexed as

Carcinoma, Non-Small-Cell LungLung Neoplasms14-3-3 ProteinsAutophagyCell Line, TumorCell ProliferationGlycogenHumansTripartite Motif ProteinsUbiquitin-Protein Ligases14-3-3 ProteinsGlycogenTRIM7 protein, humanTripartite Motif ProteinsUbiquitin-Protein LigasesAutophagyGNIP1MigrationNon-small cell lung cancerProliferation

Identifiers

PMID36042481
PMCPMC9426035
OpenAlexW4293548045

What OpenQuestion holds

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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.