Evidence map›Paper›PMID 25814666›Full record

ArticleThe Journal of biological chemistry2015

A motif from Lys216 to Lys222 in human BUB3 protein is a nuclear localization signal and critical for BUB3 function in mitotic checkpoint.

Songcheng Zhu, Ruiqi Jing, Yiwei Yang, Yitong Huang, Xin Wang, Ye Leng, Jiajie Xi, Guiying Wang, Wenwen Jia, Jiuhong Kang

Open access · hybridAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in The Journal of biological chemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.

0numbers the graph read from it
0cells of the map it votes in
5citing papers in PubMed
0.5field-weighted citation impact, top 36% 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

5 citing papers in PubMed, 6 citations in OpenAlex.

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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

10 authors at 1 institution in 1 country.

Songcheng ZhuFrom the Clinical and Translational Research Center of Shanghai First Maternity and Infant Hospital, Shanghai Key Laboratory of Signaling and Disease Research at School of Life Science and Technology, Tongji University, 1239 Si-ping Road, Shanghai 200092, China zhusongcheng@tongji.edu.cn.
Ruiqi JingFrom the Clinical and Translational Research Center of Shanghai First Maternity and Infant Hospital, Shanghai Key Laboratory of Signaling and Disease Research at School of Life Science and Technology, Tongji University, 1239 Si-ping Road, Shanghai 200092, China.
Yiwei YangFrom the Clinical and Translational Research Center of Shanghai First Maternity and Infant Hospital, Shanghai Key Laboratory of Signaling and Disease Research at School of Life Science and Technology, Tongji University, 1239 Si-ping Road, Shanghai 200092, China.
Yitong HuangFrom the Clinical and Translational Research Center of Shanghai First Maternity and Infant Hospital, Shanghai Key Laboratory of Signaling and Disease Research at School of Life Science and Technology, Tongji University, 1239 Si-ping Road, Shanghai 200092, China.
Xin WangFrom the Clinical and Translational Research Center of Shanghai First Maternity and Infant Hospital, Shanghai Key Laboratory of Signaling and Disease Research at School of Life Science and Technology, Tongji University, 1239 Si-ping Road, Shanghai 200092, China.
Ye LengFrom the Clinical and Translational Research Center of Shanghai First Maternity and Infant Hospital, Shanghai Key Laboratory of Signaling and Disease Research at School of Life Science and Technology, Tongji University, 1239 Si-ping Road, Shanghai 200092, China.
Jiajie XiFrom the Clinical and Translational Research Center of Shanghai First Maternity and Infant Hospital, Shanghai Key Laboratory of Signaling and Disease Research at School of Life Science and Technology, Tongji University, 1239 Si-ping Road, Shanghai 200092, China.
Guiying WangFrom the Clinical and Translational Research Center of Shanghai First Maternity and Infant Hospital, Shanghai Key Laboratory of Signaling and Disease Research at School of Life Science and Technology, Tongji University, 1239 Si-ping Road, Shanghai 200092, China.
Wenwen JiaFrom the Clinical and Translational Research Center of Shanghai First Maternity and Infant Hospital, Shanghai Key Laboratory of Signaling and Disease Research at School of Life Science and Technology, Tongji University, 1239 Si-ping Road, Shanghai 200092, China.
Jiuhong KangFrom the Clinical and Translational Research Center of Shanghai First Maternity and Infant Hospital, Shanghai Key Laboratory of Signaling and Disease Research at School of Life Science and Technology, Tongji University, 1239 Si-ping Road, Shanghai 200092, China jhkang@tongji.edu.cn.
Tongji University · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Human BUB3 is a key mitotic checkpoint factor that recognizes centromeric components and recruits other mitotic checkpoint molecules to the unattached kinetochore. The key amino acid residues responsible for its localization are not yet defined. In this study, we identified a motif from Lys(216) to Lys(222) in BUB3 as its nuclear localization signal. A BUB3 mutant with deletion of this motif (Del216-222) was found to localize to both the cytoplasm and the nucleus, distinct from the exclusively nuclear distribution of wild-type BUB3. Further analysis revealed that residues Glu(213), Lys(216), Lys(217), Lys(218), Tyr(219), and Phe(221), but not Lys(222), contribute to nuclear localization. Interestingly, the nuclear localization signal was also critical for the kinetochore localization of BUB3. The deletion mutant Del216-222 and a subtle mutant with four residue changes in this region (E213Q/K216E/K217E/K218E (QE)) did not localize to the kinetochore efficiently or mediate mitotic checkpoint arrest. Protein interaction data suggested that the QE mutant was able to interact with BUB1, MAD2, and BubR1 but that its association with the centromeric components CENP-A and KNL1 was impaired. A motif from Leu(61) to Leu(65) in CENP-A was found to be involved in the association of BUB3 and CENP-A in cells; however, further assays suggested that CENP-A does not physically interact with BUB3 and does not affect BUB3 localization. Our findings help to dissect the mechanisms of BUB3 in mitotic checkpoint signaling.

Indexed as

LysineM Phase Cell Cycle CheckpointsNuclear Localization SignalsActive Transport, Cell NucleusAmino Acid MotifsAmino Acid SequenceAutoantigensCell Cycle ProteinsCentromere Protein AChromosomal Proteins, Non-HistoneHEK293 CellsHeLa CellsHumansKinetochoresMolecular Sequence DataMutationAutoantigensBUB3 protein, humanCell Cycle ProteinsCENPA protein, humanCentromere Protein AChromosomal Proteins, Non-HistoneLysineNuclear Localization SignalsPoly-ADP-Ribose Binding ProteinsBUB3 (Budding Uninhibited by Benzimidazole)Cell SignalingCentromeric Protein A (CENP-A)KinetochoreKinetochore LocalizationMitotic CheckpointMitotic SpindleNuclear LocalizationProtein MotifProtein Translocation

Identifiers

PMID25814666
PMCPMC4416835
OpenAlexW2043911932

What OpenQuestion holds

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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.