Evidence map›Paper›PMID 24552808›Full record

ArticleCell cycle (Georgetown, Tex.)2014

CYLD coordinates with EB1 to regulate microtubule dynamics and cell migration.

Dengwen Li, Jinmin Gao, Yunfan Yang, Lei Sun, Shaojun Suo, Youguang Luo, Wenqing Shui, Jun Zhou, Min Liu

Open access · bronzeAbstract read
In one paragraph

Article in Cell cycle (Georgetown, Tex.), 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
3.1field-weighted citation impact, top 8% 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

21 citing papers in PubMed, 31 citations in OpenAlex.

  1. Review
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  5. Review
  6. [Research progress of deubiquitinating enzyme CYLD to regulate liver-related diseases].Zhonghua gan zang bing za zhi = Zhonghua ganzangbing zazhi = Chinese journal of hepatology · 2019
    Review
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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

9 authors at 4 institutions in 1 country.

Dengwen LiState Key Laboratory of Medicinal Chemical Biology; College of Life Sciences; Nankai University; Tianjin, China.
Jinmin GaoState Key Laboratory of Medicinal Chemical Biology; College of Life Sciences; Nankai University; Tianjin, China.
Yunfan YangState Key Laboratory of Medicinal Chemical Biology; College of Life Sciences; Nankai University; Tianjin, China.
Lei SunTianjin Key Laboratory of Medical Epigenetics; School of Basic Medical Sciences; Tianjin Medical University; Tianjin, China.
Shaojun SuoState Key Laboratory of Medicinal Chemical Biology; College of Life Sciences; Nankai University; Tianjin, China.
Youguang LuoState Key Laboratory of Medicinal Chemical Biology; College of Life Sciences; Nankai University; Tianjin, China.
Wenqing ShuiState Key Laboratory of Medicinal Chemical Biology; College of Life Sciences; Nankai University; Tianjin, China.
Jun ZhouState Key Laboratory of Medicinal Chemical Biology; College of Life Sciences; Nankai University; Tianjin, China.
Min LiuTianjin Key Laboratory of Medical Epigenetics; School of Basic Medical Sciences; Tianjin Medical University; Tianjin, China.
Nankai University · CNState Key Laboratory of Medicinal Chemical BiologyTianjin Medical University · CNState Key Laboratory of Chemical Engineering · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Cylindromatosis (CYLD), a deubiquitinase involved in inflammation and tumorigenesis via the modulation of cell signaling, has recently been identified as a critical regulator of microtubule dynamics. CYLD has also been shown to stimulate cell migration and thereby contribute to normal physiological processes. However, it remains elusive how the regulation of microtubule dynamic properties by CYLD is connected to its role in mediating cell migration. In this study, we performed yeast 2-hybrid screening with CYLD as bait and identified 7 CYLD-interacting proteins, including end-binding protein 1 (EB1). The CYLD-EB1 interaction was confirmed both in cells and in vitro, and these 2 proteins colocalized at the plus ends of microtubules. Interestingly, the association of CYLD with EB1 was significantly increased upon the stimulation of cell migration. CYLD coordinated with EB1 to orchestrate tail retraction, centrosome reorientation, and leading-edge microtubule stabilization in migratory cells. In addition, CYLD acted in concert with EB1 to regulate microtubule assembly in vitro, microtubule nucleation at the centrosome, and microtubule growth at the cell periphery. These data provide mechanistic insights into the actions of CYLD in the regulation of microtubule dynamics and cell migration. These findings also support the notion that coordinated actions of microtubule-binding proteins are critical for microtubule-mediated cellular events.

Indexed as

Cell MovementCentrosomeDeubiquitinating Enzyme CYLDHeLa CellsHumansMicrotubule-Associated ProteinsMicrotubulesTumor Suppressor ProteinsCYLD protein, humanDeubiquitinating Enzyme CYLDMAPRE1 protein, humanMicrotubule-Associated ProteinsTumor Suppressor Proteinscell migrationcentrosomeCYLDEB1microtubuleyeast-two hybrid

Identifiers

PMID24552808
PMCPMC3984320
OpenAlexW2061516335

What OpenQuestion holds

Textmetadata
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.