Evidence map›Paper›PMID 30504065›Full record

ArticleNeoplasia (New York, N.Y.)2019

PKCζ Phosphorylates SIRT6 to Mediate Fatty Acid β-Oxidation in Colon Cancer Cells.

Tian Gao, Meiting Li, Guanqun Mu, Tianyun Hou, Wei-Guo Zhu, Yang Yang

Open access · goldAbstract read
In one paragraph

Article in Neoplasia (New York, N.Y.), 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed, 1 pooled it
1.4field-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

19 citing papers in PubMed, 1 synthesis or guideline pooled it, 33 citations in OpenAlex.

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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

6 authors at 2 institutions in 1 country.

Tian GaoDepartment of Biochemistry and Molecular Biology, School of Basic Medical Sciences, Peking University Health Science Center, 38 Xueyuan Road, Beijing 100191, China.
Meiting LiDepartment of Biochemistry and Molecular Biology, School of Basic Medical Sciences, Peking University Health Science Center, 38 Xueyuan Road, Beijing 100191, China.
Guanqun MuDepartment of Biochemistry and Molecular Biology, School of Basic Medical Sciences, Peking University Health Science Center, 38 Xueyuan Road, Beijing 100191, China.
Tianyun HouDepartment of Biochemistry and Molecular Biology, School of Basic Medical Sciences, Peking University Health Science Center, 38 Xueyuan Road, Beijing 100191, China.
Wei-Guo ZhuDepartment of Biochemistry and Molecular Biology, School of Basic Medical Sciences, Peking University Health Science Center, 38 Xueyuan Road, Beijing 100191, China; Guangdong Key Laboratory for Genome Stability and Human Disease Prevention, Department of Biochemistry and Molecular Biology, School of Medicine, Shenzhen University, Shenzhen 516080, China.
Yang YangDepartment of Biochemistry and Molecular Biology, School of Basic Medical Sciences, Peking University Health Science Center, 38 Xueyuan Road, Beijing 100191, China. Electronic address: yangsh@bjmu.edu.cn.
Peking University · CNShenzhen University · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Protein kinase C (PKC) has critical roles in regulating lipid anabolism and catabolism. PKCζ, a member of atypical PKC family, has been reported to mediate glucose metabolism. However, whether and how PKCζ regulates tumor cells fatty acid β-oxidation are unknown. Here, we report that the phosphorylation of SIRT6 is significantly increased after palmitic acid (PA) treatment in colon cancer cells. PKCζ can physically interact with SIRT6 in vitro and in vivo, and this interaction enhances following PA treatment. Further experiments show that PKCζ is the phosphorylase of SIRT6 and phosphorylates SIRT6 at threonine 294 residue to promote SIRT6 enrichment on chromatin. In the functional study, we find that the expression of ACSL1, CPT1, CACT, and HADHB, the genes related to fatty acid β-oxidation, increases after PA stimulation. We further confirm that PKCζ mediates the binding of SIRT6 specifically to the promoters of fatty acid β-oxidation-related genes and elicits the expression of these genes through SIRT6 phosphorylation. Our findings demonstrate the mechanism of PKCζ as a new phosphorylase of SIRT6 on maintaining tumor fatty acid β-oxidation and define the new role of PKCζ in lipid homeostasis.

Indexed as

Oxidation-ReductionCell Line, TumorChromatinColonic NeoplasmsFatty AcidsGene Expression Regulation, NeoplasticHumansPhosphorylationProtein BindingProtein Kinase CProtein Kinase C zetaSirtuinsChromatinFatty AcidsProtein Kinase CProtein Kinase C zetaSIRT6 protein, humanSirtuins

Identifiers

PMID30504065
PMCPMC6277223
OpenAlexW2902510443

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.