Evidence map›Paper›PMID 26317901›Full record

ArticleOncotarget2015

PIWIL1 destabilizes microtubule by suppressing phosphorylation at Ser16 and RLIM-mediated degradation of Stathmin1.

Chao Li, Xiaoyan Zhou, Jianhui Chen, Yilu Lu, Qianqian Sun, Dachang Tao, Wei Hu, Xulei Zheng, Shasha Bian, Yunqiang Liu and 1 more

Open access · diamondAbstract read
In one paragraph

Article in Oncotarget, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
3.1field-weighted citation impact, top 9% 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

14 citing papers in PubMed, 21 citations in OpenAlex.

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  14. World journal of gastroenterology · 2018
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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

11 authors at 2 institutions in 1 country.

Chao LiDepartment of Medical Genetics, State Key Laboratory of Biotherapy, West China Hospital, Sichuan University, Chengdu, China.
Xiaoyan ZhouDepartment of Medical Genetics, State Key Laboratory of Biotherapy, West China Hospital, Sichuan University, Chengdu, China.
Jianhui ChenDepartment of Medical Genetics, State Key Laboratory of Biotherapy, West China Hospital, Sichuan University, Chengdu, China.
Yilu LuDepartment of Medical Genetics, State Key Laboratory of Biotherapy, West China Hospital, Sichuan University, Chengdu, China.
Qianqian SunDepartment of Medical Genetics, State Key Laboratory of Biotherapy, West China Hospital, Sichuan University, Chengdu, China.
Dachang TaoDepartment of Medical Genetics, State Key Laboratory of Biotherapy, West China Hospital, Sichuan University, Chengdu, China.
Wei HuDepartment of Medical Genetics, State Key Laboratory of Biotherapy, West China Hospital, Sichuan University, Chengdu, China.
Xulei ZhengDepartment of Medical Genetics, State Key Laboratory of Biotherapy, West China Hospital, Sichuan University, Chengdu, China.
Shasha BianDepartment of Medical Genetics, State Key Laboratory of Biotherapy, West China Hospital, Sichuan University, Chengdu, China.
Yunqiang LiuDepartment of Medical Genetics, State Key Laboratory of Biotherapy, West China Hospital, Sichuan University, Chengdu, China.
Yongxin MaDepartment of Medical Genetics, State Key Laboratory of Biotherapy, West China Hospital, Sichuan University, Chengdu, China.
Sichuan University · CNState Key Laboratory of Biotherapy

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Human PIWIL1, alias HIWI, is a member of Piwi protein family and expressed in various tumors. However, the underlying mechanism of PIWIL1 in tumorigenesis remains largely unknown. Stathmin1 is a cytosolic phosphoprotein which has a critical role in regulating microtubule dynamics and is overexpressed in many cancers. Here we report that PIWIL1 can directly bind to Stathmin1. Meanwhile, PIWIL1 can up-regulate the expression of Stathmin1 through inhibiting ubiquitin-mediated degradation induced by an E3 ubiquitin ligase RLIM. Furthermore, PIWIL1 can also reduce phosphorylation level of Stathmin1 at Ser-16 through inhibiting the interaction between CaMKII and Stathmin1. Our results showed that PIWIL1 suppresses microtubule polymerization, and promotes cell proliferation and migration via Stathmin1 for the first time. Our study reveals a novel mechanism for PIWIL1 in tumorigenesis.

Indexed as

Argonaute ProteinsBlotting, WesternCarcinogenesisCell Line, TumorCell MovementCell ProliferationFluorescent Antibody TechniqueGene Expression Regulation, NeoplasticHumansImmunoprecipitationMicrotubulesNeoplasm InvasivenessNeoplasmsPhosphorylationReal-Time Polymerase Chain ReactionSerineArgonaute ProteinsPIWIL1 protein, humanRLIM protein, humanSerineStathminSTMN1 protein, humanUbiquitin-Protein LigasesmigrationPIWIL1proliferationSTMN1tubulin

Identifiers

PMID26317901
PMCPMC4695026
OpenAlexW2130807449

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.