Evidence map›Paper›PMID 2686979›Full record

ArticleThe EMBO journal1989

Modification of nuclear lamin proteins by a mevalonic acid derivative occurs in reticulocyte lysates and requires the cysteine residue of the C-terminal CXXM motif.

K Vorburger, G T Kitten, E A Nigg

Abstract readComparative Study
In one paragraph

Article in The EMBO journal, 1989. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 65 papers.

0numbers the graph read from it
0cells of the map it votes in
65citing papers in PubMed
9.8field-weighted citation impact, top 2% 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

65 citing papers in PubMed, 185 citations in OpenAlex.

  1. Review
  2. Article
  3. Enhanced Expression of a Novel Lamin A/C Splice Variant in Idiopathic Pulmonary Fibrosis Lung.American journal of respiratory cell and molecular biology · 2023
    Article
  4. Post-Translational Modification of Lamins: Mechanisms and Functions.Frontiers in cell and developmental biology · 2022
    Review
  5. Review
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Efficient farnesylation of an extended C-terminal C(The Journal of biological chemistry · 2018
    Article
  12. Article
  13. Article
  14. 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
  15. Review
  16. Protein farnesylation and disease.Journal of inherited metabolic disease · 2012
    Review
  17. Article
  18. Article
  19. Nuclear lamins.Cold Spring Harbor perspectives in biology · 2010
    Review
  20. Article

5 more citing papers are in PubMed but not listed here.

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.

K VorburgerInstitute for Cell Biology, ETH, Zurich, Switzerland.
G T Kitten
E A Nigg
ETH Zurich · CH

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The C-terminus of nuclear lamins (CXXM) resembles a C-terminal motif (the CAAX box) of fungal mating factors and ras-related proteins. The CAAX box is subject to different types of post-translational modifications, including proteolytic processing, isoprenylation and carboxyl methylation. By peptide mapping we show that both chicken lamins A and B2 are processed proteolytically in vivo. However, whereas the entire CXXM motif is cleaved from lamin A, at most three C-terminal amino acids are removed from lamin B2. Following translation of cDNA-derived RNAs in reticulocyte lysates, lamin proteins specifically incorporate a derivative of [14C]mevalonic acid (MV), i.e. the precursor of a putative isoprenoid modification. Remarkably, no MV is incorporated into lamin B2 translated from a mutant cDNA encoding alanine instead of cysteine in the C-terminal CXXM motif. These results implicate this particular cysteine residue as the target for modification of lamin proteins by an isoprenoid MV derivative, and they indicate that isoprenylation is amenable to studies in cell-free systems. Moreover, our observations suggest that C-terminal processing of newly synthesized nuclear lamins is a multi-step process highly reminiscent of the pathway elaborated recently for ras-related proteins.

Indexed as

CysteineLamin Type BProtein Processing, Post-TranslationalAnimalsCell-Free SystemCells, CulturedChick EmbryoDNAFibroblastsLaminsLamin Type AMevalonic AcidMutationNuclear ProteinsPeptide MappingProtein BiosynthesisCysteineDNALaminsLamin Type ALamin Type BMevalonic AcidNuclear ProteinsProtein-Tyrosine KinasesProto-Oncogene ProteinsProto-Oncogene Proteins p21(ras)

Identifiers

PMID2686979
PMCPMC401575
OpenAlexW254147912

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.