Evidence map›Paper›PMID 16809321›Full record

ArticleJournal of virology2006

Localization of ERK/MAP kinase is regulated by the alphaherpesvirus tegument protein Us2.

Mathew G Lyman, Jessica A Randall, Christine M Calton, Bruce W Banfield

Open access · greenAbstract read
In one paragraph

Article in Journal of virology, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
0.4field-weighted citation impact, top 32% 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

18 citing papers in PubMed, 29 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Review
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. A common neuronal response to alphaherpesvirus infection.Journal of neuroimmune pharmacology : the official journal of the Society on NeuroImmune Pharmacology · 2010
    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

4 authors at 1 institution in 1 country.

Mathew G LymanDepartment of Microbiology, University of Colorado at Denver and Health Sciences Center, Mail Stop 8333, P.O. Box 6511, Aurora, 80045, USA.
Jessica A Randall
Christine M Calton
Bruce W Banfield
University of Colorado Denver · US

Funding

Modulation of cell signaling pathways by alphaherpesvirus tegument componentsR01AI048626 · NIAID · UNIVERSITY OF COLORADO DENVER · PI BANFIELD, BRUCE W · 2001 to 2011
$2.5M
Molecular Pathogenesis of Infectious DiseasesT32AI052066 · NIAID · UNIVERSITY OF COLORADO DENVER · PI VAN DYK, LINDA F. · 2002 to 2022
$2.3M
NIAID NIH HHS AI48626NIAID NIH HHS AI52066NIAID NIH HHS R01 AI048626NIAID NIH HHS T32 AI052066
6 · The paper itself

Abstract

Many different viruses activate the extracellular signal-regulated kinase (ERK)/mitogen-activated protein (MAP) kinase signaling pathway during infection and require ERK activation for the efficient execution of their replication programs. Despite these findings, no virus-encoded proteins have been identified that directly modulate ERK activities. In an effort to determine the function of a conserved alphaherpesvirus structural protein called Us2, we screened a yeast two-hybrid library derived from NIH 3T3 cells and identified ERK as a Us2-interacting protein. Our studies indicate that Us2 binds to ERK in virus-infected cells, mediates the incorporation of ERK into the virion, and inhibits the activation of ERK nuclear substrates. The association of Us2 with ERK leads to the sequestration of ERK at the plasma membrane and to a perinuclear vesicular compartment, thereby keeping ERK out of the nucleus. Us2 can bind to activated ERK, and the data suggest that Us2 does not inhibit ERK enzymatic activity. The treatment of cells with U0126, a specific inhibitor of ERK activation, resulted in a substantial delay in the release of virus from infected cells that was more pronounced with a virus deleted for Us2 than with parental and repaired strains, suggesting that both ERK and Us2 activities are required for efficient virus replication. This study highlights an additional complexity to the activation of ERK by viruses, namely, that localization of active ERK can be altered by virus-encoded proteins.

Indexed as

AnimalsBase SequenceButadienesCell MembraneCytoplasmic VesiclesEnzyme ActivationEnzyme InhibitorsExtracellular Signal-Regulated MAP KinasesHerpesvirus 1, SuidHumansMiceNIH 3T3 CellsNitrilesProtein TransportPseudorabiesSequence DeletionButadienesEnzyme InhibitorsExtracellular Signal-Regulated MAP KinasesNitrilesU 0126Viral Envelope Proteins

Identifiers

PMID16809321
PMCPMC1489020
OpenAlexW2070089640

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.