Evidence map›Paper›PMID 23318443›Full record

ArticleOncogene2014

Kaposi's sarcoma-associated herpesvirus lana2 protein interacts with the pocket proteins and inhibits their sumoylation.

L Marcos-Villar, P Gallego, C Muñoz-Fontela, C F de la Cruz-Herrera, M Campagna, D González, F Lopitz-Otsoa, M S Rodríguez, C Rivas

Open access · bronzeAbstract read
PubMed Publisher
In one paragraph

Article in Oncogene, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
1.1field-weighted citation impact, top 22% 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

14 citing papers in PubMed, 20 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Metabolic Control by DNA Tumor Virus-Encoded Proteins.Pathogens (Basel, Switzerland) · 2021
    Review
  5. Review
  6. Article
  7. Article
  8. Viral Interplay with the Host Sumoylation System.Advances in experimental medicine and biology · 2017
    Review
  9. Review
  10. Review
  11. Article
  12. Article
  13. Review
  14. Review
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

9 authors at 3 institutions in 2 countries.

L Marcos-VillarCentro Nacional de Biotecnología, CSIC, Campus Universidad Autónoma de Madrid, Madrid, Spain.
P GallegoCentro Nacional de Biotecnología, CSIC, Campus Universidad Autónoma de Madrid, Madrid, Spain.
C Muñoz-FontelaHeinrich Pette Institute, Leibniz Institute for Experimental Virology, Hamburg, Germany.
C F de la Cruz-HerreraCentro Nacional de Biotecnología, CSIC, Campus Universidad Autónoma de Madrid, Madrid, Spain.
M CampagnaCentro Nacional de Biotecnología, CSIC, Campus Universidad Autónoma de Madrid, Madrid, Spain.
D GonzálezCentro Nacional de Biotecnología, CSIC, Campus Universidad Autónoma de Madrid, Madrid, Spain.
F Lopitz-OtsoaProteomics Unit, CIC bioGUNE, CIBERehd, Bizkaia Technology Park, Buildin Derio, Spain.
M S Rodríguez1] Proteomics Unit, CIC bioGUNE, CIBERehd, Bizkaia Technology Park, Buildin Derio, Spain [2] Ubiquitylation and Cancer Molecular Biology laboratory, Inbiomed, San Sebastian-Donostia, Gipuzkoa, Spain.
C RivasCentro Nacional de Biotecnología, CSIC, Campus Universidad Autónoma de Madrid, Madrid, Spain.
Universidad Autónoma de Madrid · ESCentro Nacional de Biotecnología · ESLeibniz Institute of Virology (LIV) · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The pocket proteins retinoblastoma protein (pRb), p107 and p130 are the key targets of oncoproteins expressed by DNA tumor viruses. Some of these viral proteins contain an LXCXE motif that mediates the interaction with the three pocket proteins and the inhibition of the pRb SUMOylation. Kaposi's sarcoma herpesvirus (KSHV) contains at least two proteins that can regulate pRb function but, so far, a KSHV-encoded protein targeting p107 and p130 has not been identified. Here, we show that the KSHV latent protein LANA2 binds to pRb, p107 and p130. LANA2 contains an LXCXE motif that is required for bypassing pRb-mediated cell-cycle arrest and for inhibiting pRb SUMOylation. Finally, we demonstrate that, in addition to pRb, both p107 and p130 can be SUMOylated, and this modification is also inhibited by LANA2 in an LXCXE-dependent manner. These results demonstrate, for the first time, the SUMOylation of p107 or p130 and, so far, they represent the first example of a KSHV protein able to interact with the three pocket proteins and to inhibit their conjugation to SUMO.

Indexed as

SumoylationBlotting, WesternCell Line, TumorCrk-Associated Substrate ProteinHerpesvirus 8, HumanHumansImmunoprecipitationInterferon Regulatory FactorsRetinoblastoma-Like Protein p107Retinoblastoma ProteinViral ProteinsBCAR1 protein, humanCrk-Associated Substrate ProteinInterferon Regulatory FactorsRBL1 protein, humanRetinoblastoma-Like Protein p107Retinoblastoma Proteinviral interferon regulatory factorsViral Proteins

Identifiers

PMID23318443
OpenAlexW2094563986

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.