Evidence map›Paper›PMID 8978814›Full record

ArticleThe Journal of cell biology1996

Lamin proteolysis facilitates nuclear events during apoptosis.

L Rao, D Perez, E White

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of cell biology, 1996. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 152 papers.

0numbers the graph read from it
0cells of the map it votes in
152citing papers in PubMed
23.6field-weighted citation impact, top 1% 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

152 citing papers in PubMed, 580 citations in OpenAlex.

  1. Review
  2. Hyperactive Rac converts sublethal to lethal trogocytosis in vivo.Proceedings of the National Academy of Sciences of the United States of America · 2026
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  4. Hyperactive Rac converts sublethal nibbling to lethal phagocytosisbioRxiv : the preprint server for biology · 2025
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  5. Cells · 2025
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  11. Review
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  13. Review
  14. Review
  15. eIF5A-Independent Role of DHPS in p21International journal of molecular sciences · 2021
    Article
  16. Article
  17. Orchestration of Force Generation and Nuclear Collapse in Apoptotic Cells.International journal of molecular sciences · 2021
    Review
  18. Article
  19. Article
  20. Article

92 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.

L RaoCenter for Advanced Biotechnology and Medicine, Cancer Institute of New Jersey, Piscataway 08854, USA.
D Perez
E White
Beth Mardutho · US

Funding

Function of the Adenovirus E1B OncogeneR37CA053370 · NCI · RUTGERS THE ST UNIV OF NJ NEW BRUNSWICK · PI WHITE, EILEEN P. · 2001 to 2009
$3.1M
FUNCTION OF THE ADENOVIRUS E1B ONCOGENER01CA053370 · NCI · RUTGERS THE ST UNIV OF NJ NEW BRUNSWICK · PI WHITE, EILEEN · 1991 to 2000
$195k
NCI NIH HHS CA53370
6 · The paper itself

Abstract

Expression of the adenovirus E1A oncogene stimulates both cell proliferation and p53-dependent apoptosis in rodent cells. p53 implements apoptosis in all or in part through transcriptional activation of bax, the product of which promotes cell death. The adenovirus E1B 19K product is homologous in sequence and in function to Bcl-2, both of which bind to and inhibit the activity of Bax and thereby suppress apoptosis. The E1B 19K protein also interacts with the nuclear lamins, but the role of this interaction in the regulation of apoptosis is not known. Lamins are, however, substrates for members of the interleukin-1 beta-converting enzyme (ICE) family of cysteine proteases that are activated during apoptosis and function downstream of Bcl-2 in the cell death pathway. lamins are degraded during E1A-induced p53-dependent apoptosis. Lamin A and C are cleaved into 47- and 37-kD fragments, respectively, and the site of proteolysis is mapped to a conserved aspartic acid residue at position 230. The cleavage of lamins during apoptosis is consistent with the activation of an ICE-related cysteine protease down-stream of p53. No lamin protease activity was detected in cells expressing the E1B 19K protein, indicating that 19K functions upstream of protease activation in inhibiting apoptosis. Substitution of the aspartic acid at the cleavage site produced a mutant lamin protein that was resistant to proteolysis both in vitro and in vivo. Expression of uncleavable mutant lamin A or B attenuated apoptosis, delaying cell death and the associated DNA fragmentation by 12 h. Mutant lamin expressing cells failed to show the signs of chromatin condensation and nuclear shrinkage typical of cell death by apoptosis. Instead, the nuclear envelope collapsed and the nuclear lamina remained intact. However, the late stage of apoptosis was morphologically unaltered and formation of apoptotic bodies was evident. Thus, lamin breakdown by proteolytic degradation facilitates the nuclear events of apoptosis perhaps by facilitating nuclear breakdown.

Indexed as

Adenovirus E1B ProteinsAmino Acid SequenceAnimalsApoptosisBinding SitesCaspase 1Cell LineCell NucleusCysteine EndopeptidasesDNA FragmentationEndopeptidasesEnzyme ActivationHeLa CellsHumansKineticsLaminsAdenovirus E1B ProteinsCaspase 1Cysteine EndopeptidasesEndopeptidasesLaminsLamin Type ANuclear ProteinsTumor Suppressor Protein p53

Identifiers

PMID8978814
PMCPMC2133948
OpenAlexW2074678011

What OpenQuestion holds

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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.