Evidence map›Paper›PMID 20675372›Full record

ArticleThe Journal of biological chemistry2010

The L279P mutation of nuclear distribution gene C (NudC) influences its chaperone activity and lissencephaly protein 1 (LIS1) stability.

Xiao-Jing Zhu, Xunyan Liu, Qi Jin, Yuqi Cai, Yuehong Yang, Tianhua Zhou

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.

0numbers the graph read from it
0cells of the map it votes in
26citing papers in PubMed
1.5field-weighted citation impact, top 19% 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

26 citing papers in PubMed, 42 citations in OpenAlex.

  1. Article
  2. Review
  3. Review
  4. Review
  5. Article
  6. Editorial: Editor's Pick 2021: Highlights in Cell Adhesion and Migration.Frontiers in cell and developmental biology · 2022
    Article
  7. PCID2, a subunit of theRNA biology · 2021
    Article
  8. Article
  9. Article
  10. Review
  11. Article
  12. Overexpression of theFrontiers in plant science · 2020
    Article
  13. NudC regulates photoreceptor disk morphogenesis and rhodopsin localization.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2019
    Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. Article
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

6 authors at 1 institution in 1 country.

Xiao-Jing ZhuDepartment of Cell Biology and Program in Molecular Cell Biology, Zhejiang University School of Medicine, Hangzhou 310058, China.
Xunyan Liu
Qi Jin
Yuqi Cai
Yuehong Yang
Tianhua Zhou
Zhejiang University · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

LIS1, a gene mutated in classical lissencephaly, plays essential roles in cytoplasmic dynein regulation, mitosis and cell migration. However, the regulation of LIS1 (lissencephaly protein 1) protein remains largely unknown. Genetic studies in Aspergillus nidulans have uncovered that the Nud (nuclear distribution) pathway is involved in the regulation of cytoplasmic dynein complex and a temperature-sensitive mutation in the nudC gene (L146P) greatly reduces the protein levels of NudF, an Aspergillus ortholog of LIS1. Here, we showed that L146 in Aspergillus NudC and its flanking region were highly conservative during evolution. The similar mutation in human NudC (L279P) obviously led to reduced LIS1 and cellular phenotypes similar to those of LIS1 down-regulation. To explore the underlying mechanism, we found that the p23 domain-containing protein NudC bound to the molecular chaperone Hsp90, which is also associated with LIS1. Inhibition of Hsp90 chaperone function by either geldanamycin or radicicol resulted in a decrease in LIS1 levels. Ectopic expression of Hsp90 partially reversed the degradation of LIS1 caused by overexpression of NudC-L279P. Furthermore, NudC was found to regulate the ATPase activity of Hsp90, which was repressed by the mutation of L279P. Interestingly, NudC itself was shown to possess a chaperone function, which also was suppressed by the L279P mutation. Together, these data suggest that NudC may be involved in the regulation of LIS1 stability by its chaperone function.

Indexed as

Mutation, Missense1-Alkyl-2-acetylglycerophosphocholine EsteraseAmino Acid SubstitutionAnimalsAspergillus nidulansBenzoquinonesCell Cycle ProteinsDrosophila melanogasterEnzyme InhibitorsEnzyme StabilityHeLa CellsHSP90 Heat-Shock ProteinsHumansLactams, MacrocyclicMacrolidesMice1-Alkyl-2-acetylglycerophosphocholine EsteraseBenzoquinonesCell Cycle ProteinsEnzyme InhibitorsgeldanamycinHSP90 Heat-Shock ProteinsLactams, MacrocyclicMacrolidesMicrotubule-Associated ProteinsmonordenNuclear ProteinsNUDC protein, humanPAFAH1B1 protein, human

Identifiers

PMID20675372
PMCPMC2943274
OpenAlexW2082478189

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.