Evidence map›Paper›PMID 2808518›Full record

ArticleThe Journal of cell biology1989

The conserved carboxy-terminal cysteine of nuclear lamins is essential for lamin association with the nuclear envelope.

G Krohne, I Waizenegger, T H Höger

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of cell biology, 1989. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 53 papers.

0numbers the graph read from it
0cells of the map it votes in
53citing papers in PubMed
6.0field-weighted citation impact, top 3% 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

53 citing papers in PubMed, 132 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Farnesylation of lamin B1 is important for retention of nuclear chromatin during neuronal migration.Proceedings of the National Academy of Sciences of the United States of America · 2013
    Article
  6. Protein farnesylation and disease.Journal of inherited metabolic disease · 2012
    Review
  7. Epigenetic alterations in muscular disorders.Comparative and functional genomics · 2012
    Article
  8. Article
  9. Review
  10. Hutchinson-Gilford progeria mutant lamin A primarily targets human vascular cells as detected by an anti-Lamin A G608G antibody.Proceedings of the National Academy of Sciences of the United States of America · 2006
    Article
  11. Article
  12. Article
  13. Article
  14. Meiotic lamin C2: the unique amino-terminal hexapeptide GNAEGR is essential for nuclear envelope association.Proceedings of the National Academy of Sciences of the United States of America · 2000
    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

3 authors at 1 institution in 1 country.

G KrohneDivision of Membrane Biology and Biochemistry, German Cancer Research Center, Heidelberg.
I Waizenegger
T H Höger
German Cancer Research Center · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

We have analyzed the interaction of soluble nuclear lamins with the nuclear envelope by microinjection of normal and mutated lamins into the cytoplasm of Xenopus laevis oocytes. Our results demonstrate that the conserved cysteine of the carboxy-terminal tetrapeptide Cys Ala/Ser Ile Met of lamins is essential for their association with the nuclear envelope. Removal of this sequence or replacement of the cysteine by serine resulted in Xenopus lamin L1 remaining in a soluble, non-envelope-associated state within the nucleus. Similar mutations of Xenopus lamin A resulted in only partial reduction of nuclear envelope association, indicating that lamin A contains additional signals that can partially compensate for the lack of the cysteine. Mammalian lamin C lacks this tetrapeptide and is not associated with the nuclear envelope in our experimental system. Cloning of the tetrapeptide Cys Ala Ile Met to the carboxy terminus of human lamin C resulted in lamin being found in a nuclear envelope-associated form in oocytes. Mutations at the amino terminus and in the alpha-helical region of lamin L1 revealed that the carboxy terminus mediates the association of lamins with the nuclear envelope; however, this alone is insufficient for maintenance of a stable association with the nuclear envelope.

Indexed as

CysteineMutationAmino Acid SequenceAnimalsAzidesChromosome DeletionFemaleLaminsLamin Type AMolecular Sequence DataNuclear EnvelopeNuclear ProteinsOocytesProtein BindingRNA, Transfer, Amino AcylXenopus laevisAzidesCysteinelamin CLaminsLamin Type ANuclear ProteinsRNA, Transfer, Amino AcyltRNA, 2-nitro-5-azidobenzoyllysine-

Identifiers

PMID2808518
PMCPMC2115888
OpenAlexW2097325653

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
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.