Evidence map›Paper›PMID 28516914›Full record

ArticleNature communications2017

Adenylate kinase hCINAP determines self-renewal of colorectal cancer stem cells by facilitating LDHA phosphorylation.

Yapeng Ji, Chuanzhen Yang, Zefang Tang, Yongfeng Yang, Yonglu Tian, Hongwei Yao, Xi Zhu, Zeming Zhang, Jiafu Ji, Xiaofeng Zheng

Erratum issuedOpen access · goldAbstract read
In one paragraph

Article in Nature communications, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 58 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
58citing papers in PubMed, 1 pooled it
1.5field-weighted citation impact, top 20% 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

58 citing papers in PubMed, 1 synthesis or guideline pooled it, 80 citations in OpenAlex.

  1. Interplay Between Glucose Metabolism and Chromatin Modifications in Cancer.Frontiers in cell and developmental biology · 2021
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  10. Review
  11. Targeting LINC01711 in FAPCell death & disease · 2025
    Article
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  14. Review
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4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

10 authors at 3 institutions in 1 country.

Yapeng JiState Key Laboratory of Protein and Plant Gene Research, School of Life Sciences, Peking University, Beijing 100871, China.
Chuanzhen YangState Key Laboratory of Protein and Plant Gene Research, School of Life Sciences, Peking University, Beijing 100871, China.
Zefang TangBiodynamic Optical Imaging Center, School of Life Sciences, Peking University, Beijing 100871, China.
Yongfeng YangState Key Laboratory of Protein and Plant Gene Research, School of Life Sciences, Peking University, Beijing 100871, China.
Yonglu TianDepartment of Biochemistry and Molecular Biology, School of Life Sciences, Peking University, Beijing 100871, China.
Hongwei YaoDepartment of Critical Care Medicine, The Third Hospital, Peking University, Beijing 100871, China.
Xi ZhuDepartment of Critical Care Medicine, The Third Hospital, Peking University, Beijing 100871, China.
Zeming ZhangBiodynamic Optical Imaging Center, School of Life Sciences, Peking University, Beijing 100871, China.
Jiafu JiDepartment of Gastrointestinal Surgery, Key Laboratory of Carcinogenesis and Translational Research, Peking University Cancer Hospital &Institute, Beijing 100142, China.
Xiaofeng ZhengState Key Laboratory of Protein and Plant Gene Research, School of Life Sciences, Peking University, Beijing 100871, China.
Peking University · CNPeking University Cancer Hospital · CNPeking University Third Hospital · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Targeting the specific metabolic phenotypes of colorectal cancer stem cells (CRCSCs) is an innovative therapeutic strategy for colorectal cancer (CRC) patients with poor prognosis and relapse. However, the context-dependent metabolic traits of CRCSCs remain poorly elucidated. Here we report that adenylate kinase hCINAP is overexpressed in CRC tissues. Depletion of hCINAP inhibits invasion, self-renewal, tumorigenesis and chemoresistance of CRCSCs with a loss of mesenchymal signature. Mechanistically, hCINAP binds to the C-terminal domain of LDHA, the key regulator of glycolysis, and depends on its adenylate kinase activity to promote LDHA phosphorylation at tyrosine 10, resulting in the hyperactive Warburg effect and the lower cellular ROS level and conferring metabolic advantage to CRCSC invasion. Moreover, hCINAP expression is positively correlated with the level of Y10-phosphorylated LDHA in CRC patients. This study identifies hCINAP as a potent modulator of metabolic reprogramming in CRCSCs and a promising drug target for CRC invasion and metastasis.

Indexed as

Gene Expression Regulation, NeoplasticProtein Processing, Post-TranslationalAnimalsAntineoplastic AgentsCarcinogenesisColorectal NeoplasmsDNA-Binding ProteinsDoxycyclineDrug Resistance, NeoplasmGlycolysisHumansIsoenzymesLactate Dehydrogenase 5L-Lactate DehydrogenaseMiceMice, NudeAntineoplastic AgentsDNA-Binding ProteinsDoxycyclineIsoenzymesLactate Dehydrogenase 5L-Lactate DehydrogenaseNuclear ProteinsReactive Oxygen SpeciesRNA, Small InterferingTSPYL2 protein, humanTyrosine

Identifiers

PMID28516914
PMCPMC5454382
OpenAlexW2616810392

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.