Evidence map›Paper›PMID 33204722›Full record

ArticleBioMed research international2020

Revealing PAK2's Function in the Cell Division through MKLP1's Interactome.

Zhao-Huan Zhang, Xiu-Ling Liu, Yun-Yi Zhu, Hai Huang, Xiao-Hui Xu

RetractedOpen access · hybridAbstract readRetracted Publication
In one paragraph

Article in BioMed research international, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. It has been retracted, and should not be counted. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed
0.6field-weighted citation impact, top 37% 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

4 citing papers in PubMed, 6 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Tex264 Binding to SNX27 Regulates ItgBioMed research international · 2022
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4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

5 authors at 1 institution in 1 country.

Zhao-Huan Zhang *School of Life Sciences, Shanghai University, Shanghai 200444, China.ORCID https://orcid.org/0000-0001-6882-9761
Xiu-Ling Liu *School of Life Sciences, Shanghai University, Shanghai 200444, China.ORCID https://orcid.org/0000-0002-9495-3616
Yun-Yi ZhuSchool of Life Sciences, Shanghai University, Shanghai 200444, China.ORCID https://orcid.org/0000-0002-0365-8946
Hai HuangSchool of Life Sciences, Shanghai University, Shanghai 200444, China.ORCID https://orcid.org/0000-0002-5224-9911
Xiao-Hui XuSchool of Life Sciences, Shanghai University, Shanghai 200444, China.ORCID https://orcid.org/0000-0001-7608-4114
Wannan Medical College · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Cell division-related proteins are essential for the normal development and differentiation of cells and may be related to the occurrence of cancer and the drug resistance mechanism of cancer cells. The mitotic kinesin-like protein 1 (MKLP1) is a kinesin protein that has been involved in the assembly of the midzone/midbody during mitosis and cytokinesis. In this study, we found that the tail domain of MKLP1 exhibited an autoinhibitory effect on its motor activity. Overexpression of the tail domain in HEK293 cells blocked cytokinesis and caused bi-/multinucleation. It is possible that protein binding to the MKLP1 tail relieves this autoinhibition and induces the motility of MKLP1. We used the GST pull-down assay followed by the LC-MS/MS analysis and identified 54 MKLP1 tail domain-specific binding proteins. Further, we confirmed the MS result by coimmunoprecipitation and FRET that a serine/threonine kinase, p21-activated kinase 2 (PAK2), binding to MKLP1. Endogenous PAK2 expression was found to be identical to that of MKLP1 in HEK293 cells during cytokinesis. Finally, functional studies indicated that when PAK2 expression was downregulated by siRNA, MKLP1 underwent a change in its localization away from the midbody, and cell cytokinesis was subsequently impeded. This study presents a novel regulatory mechanism that PAK2 promotes the activation of MKLP1 and contributes to complete cell cytokinesis.

Indexed as

Chromatography, LiquidCytokinesisFluorescence Resonance Energy TransferHEK293 CellsHumansMicrotubule-Associated Proteinsp21-Activated KinasesProtein DomainsProtein Interaction Domains and MotifsRNA InterferenceTandem Mass SpectrometryKIF23 protein, humanMicrotubule-Associated Proteinsp21-Activated KinasesPAK2 protein, human

Identifiers

PMID33204722
PMCPMC7666706
OpenAlexW3097046034

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.