Evidence map›Paper›PMID 37083534›Full record

ArticleScience advances2023

Structural basis for CEP192-mediated regulation of centrosomal AURKA.

Jin-Gyeong Park, Hanul Jeon, Sangchul Shin, Chiman Song, Hyomin Lee, Nak-Kyoon Kim, Eunice EunKyeong Kim, Kwang Yeon Hwang, Bong-Jin Lee, In-Gyun Lee

Erratum issuedOpen access · goldAbstract read
In one paragraph

Article in Science advances, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 15 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed, 1 pooled it
4.6field-weighted citation impact, top 5% 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

15 citing papers in PubMed, 1 synthesis or guideline pooled it, 22 citations in OpenAlex.

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  15. Pentagamavunone-1 inhibits aggressive breast cancer cell proliferation through mitotic catastrophe and ROS-mediated activities:Saudi pharmaceutical journal : SPJ : the official publication of the Saudi Pharmaceutical Society · 2024
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4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

10 authors at 3 institutions in 2 countries.

Jin-Gyeong ParkBiomedical Research Division, Korea Institute of Science and Technology, Seoul 02792, South Korea.ORCID 0000-0001-8940-640X
Hanul JeonBiomedical Research Division, Korea Institute of Science and Technology, Seoul 02792, South Korea.ORCID 0000-0003-0021-0107
Sangchul ShinTechnology Support Center, Korea Institute of Science and Technology, Seoul 02792, South Korea.ORCID 0000-0003-0156-680X
Chiman SongBiomedical Research Division, Korea Institute of Science and Technology, Seoul 02792, South Korea.ORCID 0000-0002-4334-6218
Hyomin LeeDepartment of Biological Chemistry, University of Science and Technology, Daejeon 34113, South Korea.ORCID 0000-0001-9892-4831
Nak-Kyoon KimAdvanced Analysis Center, Korea Institute of Science and Technology, Seoul 02792, South Korea.ORCID 0000-0002-7707-8055
Eunice EunKyeong KimBiomedical Research Division, Korea Institute of Science and Technology, Seoul 02792, South Korea.
Kwang Yeon HwangDepartment of Biotechnology, College of Life Sciences and Biotechnology, Korea University, Seoul 02841, South Korea.ORCID 0000-0002-2076-5030
Bong-Jin LeeThe Research Institute of Pharmaceutical Sciences, College of Pharmacy, Seoul National University, Seoul 08826, South Korea.
In-Gyun LeeBiomedical Research Division, Korea Institute of Science and Technology, Seoul 02792, South Korea.ORCID 0000-0003-2813-3385
Korea Institute of Science and Technology · KRKorea University · KRNew Generation University College · ET

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Aurora kinase A (AURKA) performs critical functions in mitosis. Thus, the activity and subcellular localization of AURKA are tightly regulated and depend on diverse factors including interactions with the multiple binding cofactors. How these different cofactors regulate AURKA to elicit different levels of activity at distinct subcellular locations and times is poorly understood. Here, we identified a conserved region of CEP192, the major cofactor of AURKA, that mediates the interaction with AURKA. Quantitative binding studies were performed to map the interactions of a conserved helix (Helix-1) within CEP192. The crystal structure of Helix-1 bound to AURKA revealed a distinct binding site that is different from other cofactor proteins such as TPX2. Inhibiting the interaction between Helix-1 and AURKA in cells led to the mitotic defects, demonstrating the importance of the interaction. Collectively, we revealed a structural basis for the CEP192-mediated AURKA regulation at the centrosome, which is distinct from TPX2-mediated regulation on the spindle microtubule.

Indexed as

Aurora Kinase ASpindle ApparatusCentrosomeMicrotubulesMitosisAurora Kinase A

Identifiers

PMID37083534
PMCPMC10121170
OpenAlexW4366602663

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
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.