Evidence map›Paper›PMID 29559472›Full record

ArticleCancer research2018

Plk1-Mediated Phosphorylation of TSC1 Enhances the Efficacy of Rapamycin.

Zhiguo Li, Yifan Kong, Longzhen Song, Qian Luo, Jinghui Liu, Chen Shao, Xianzeng Hou, Xiaoqi Liu

Open access · bronzeAbstract read
In one paragraph

Article in Cancer research, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
0.9field-weighted citation impact, top 26% 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

13 citing papers in PubMed, 23 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Review
  7. Article
  8. Review
  9. Role of TSC1 in physiology and diseases.Molecular and cellular biochemistry · 2021
    Review
  10. Review
  11. Article
  12. Article
  13. Article
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 1 institution in 1 country.

Zhiguo LiDepartment of Biochemistry, Purdue University, West Lafayette, Indiana.
Yifan KongDepartment of Biochemistry, Purdue University, West Lafayette, Indiana.
Longzhen SongDepartment of Biochemistry, Purdue University, West Lafayette, Indiana.
Qian LuoDepartment of Biochemistry, Purdue University, West Lafayette, Indiana.
Jinghui LiuDepartment of Biochemistry, Purdue University, West Lafayette, Indiana.
Chen ShaoDepartment of Biochemistry, Purdue University, West Lafayette, Indiana.
Xianzeng HouDepartment of Biochemistry, Purdue University, West Lafayette, Indiana.
Xiaoqi LiuDepartment of Biochemistry, Purdue University, West Lafayette, Indiana. liu8@purdue.edu.
Purdue University West Lafayette · US

Funding

Transgenic Mouse Core Facility Shared Resource (TMCF-SR)P30CA023168 · NCI · PURDUE UNIVERSITY WEST LAFAYETTE · PI John Tesmer · 1985 to 2026
$43.4M
Plk1 in Chemo-resistance of CancerR01CA157429 · NCI · UNIVERSITY OF KENTUCKY · PI XIAOQI LIU · 2011 to 2026
$3.5M
Improving chemotherapy of castration-resistant prostate cancer.R01CA196634 · NCI · UNIVERSITY OF KENTUCKY · PI LIU, XIAOQI · 2016 to 2025
$3.3M
Treatment of Castration-resistant Prostate Cancer (CRPC)R01CA196835 · NCI · UNIVERSITY OF KENTUCKY · PI LIU, XIAOQI · 2016 to 2020
$1.7M
Enhancing anti-neoplastic activity of metformin in prostate cancerR01CA192894 · NCI · UNIVERSITY OF KENTUCKY · PI LIU, XIAOQI · 2016 to 2020
$1.7M
NCI NIH HHS P30 CA023168NCI NIH HHS R01 CA157429NCI NIH HHS R01 CA192894NCI NIH HHS R01 CA196634NCI NIH HHS R01 CA196835
6 · The paper itself

Abstract

The AKT/TSC/mTOR axis is an important pathway controlling cell growth, survival, and proliferation in response to extracellular cues. Recently, it was reported that AKT activity fluctuates across the cell cycle. However, it remains unclear whether downstream targets of AKT are also regulated by the cell cycle. Here, we report that mTORC1 activity inversely correlates with AKT activity during the cell cycle. Mechanistically, Plk1 phosphorylation of TSC1 at S467 and S578 interfered with TSC1/TSC2 binding, destabilized TSC1, promoted dissociation of the TSC complex from the lysosome, and eventually led to mTORC1 activation. Tumors derived from cancer cells expressing the TSC1-S467E/S578E mutant exhibited greater sensitivity to rapamycin than those expressing WT TSC1. Collectively, our data support a model in which Plk1, instead of AKT, regulates the TSC/mTORC1 pathway during mitosis, eventually regulating the efficacy of rapamycin.

Indexed as

AnimalsCell CycleCell Cycle ProteinsCell LineCell Line, TumorHEK293 CellsHeLa CellsHumansMicePhosphorylationPolo-Like Kinase 1Protein Serine-Threonine KinasesProto-Oncogene ProteinsProto-Oncogene Proteins c-aktSignal TransductionSirolimusCell Cycle ProteinsPolo-Like Kinase 1Protein Serine-Threonine KinasesProto-Oncogene ProteinsProto-Oncogene Proteins c-aktSirolimusTOR Serine-Threonine KinasesTSC1 protein, humanTuberous Sclerosis Complex 1 Protein

Identifiers

PMID29559472
PMCPMC5984699
OpenAlexW2792248099

What OpenQuestion holds

Textmetadata
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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.