Evidence map›Paper›PMID 19023411›Full record

ArticlePLoS pathogens2008

Role of amphipathic helix of a herpesviral protein in membrane deformation and T cell receptor downregulation.

Chan-Ki Min, Sun-Young Bang, Bon-A Cho, Yun-Hui Choi, Jae-Seong Yang, Sun-Hwa Lee, Seung-Yong Seong, Ki Woo Kim, Sanguk Kim, Jae Ung Jung and 3 more

Open access · goldAbstract read
In one paragraph

Article in PLoS pathogens, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
1.9field-weighted citation impact, top 14% 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

21 citing papers in PubMed, 29 citations in OpenAlex.

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  4. Structure of a lipid A phosphoethanolamine transferase suggests how conformational changes govern substrate binding.Proceedings of the National Academy of Sciences of the United States of America · 2017
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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

13 authors at 5 institutions in 2 countries.

Chan-Ki MinDepartment of Microbiology and Immunology, College of Medicine and Institute of Endemic Diseases, Seoul National University Medical Research Center and Bundang Hospital, Seoul, Korea.
Sun-Young Bang
Bon-A Cho
Yun-Hui Choi
Jae-Seong Yang
Sun-Hwa Lee
Seung-Yong Seong
Ki Woo Kim
Sanguk Kim
Jae Ung Jung
Myung-Sik Choi
Ik-Sang Kim
Nam-Hyuk Cho
Seoul National University Bundang Hospital · KRPohang University of Science and Technology · KRSeoul National University · KRSeoul National University Hospital · KRUniversity of Southern California · US

Funding

MOLECULAR BASIS FOR HERPESVIRUS SAIMIRI ONCOGENICITYR01CA031363 · NCI · UNIVERSITY OF SOUTHERN CALIFORNIA · PI JUNG, JAE U · 1985 to 2014
$4.9M
Herpesvirus saimiri TIPR01CA109697 · NCI · UNIVERSITY OF SOUTHERN CALIFORNIA · PI JUNG, JAE U · 2005 to 2009
$1.5M
NCI NIH HHS CA109697NCI NIH HHS CA31363NCI NIH HHS R01 CA031363NCI NIH HHS R01 CA109697
6 · The paper itself

Abstract

Lipid rafts are membrane microdomains that function as platforms for signal transduction and membrane trafficking. Tyrosine kinase interacting protein (Tip) of T lymphotropic Herpesvirus saimiri (HVS) is targeted to lipid rafts in T cells and downregulates TCR and CD4 surface expression. Here, we report that the membrane-proximal amphipathic helix preceding Tip's transmembrane (TM) domain mediates lipid raft localization and membrane deformation. In turn, this motif directs Tip's lysosomal trafficking and selective TCR downregulation. The amphipathic helix binds to the negatively charged lipids and induces liposome tubulation, the TM domain mediates oligomerization, and cooperation of the membrane-proximal helix with the TM domain is sufficient for localization to lipid rafts and lysosomal compartments, especially the mutivesicular bodies. These findings suggest that the membrane-proximal amphipathic helix and TM domain provide HVS Tip with the unique ability to deform the cellular membranes in lipid rafts and to downregulate TCRs potentially through MVB formation.

Indexed as

CD4 AntigensCell MembraneDown-RegulationHerpesvirus 2, SaimiriineHumansJurkat CellsLipidsLysosomesMembrane MicrodomainsPhosphoproteinsProtein Structure, SecondaryReceptors, Antigen, T-CellT-LymphocytesViral ProteinsCD4 AntigensLipidsPhosphoproteinsReceptors, Antigen, T-Celltyrosine kinase interacting protein, Saimiriine herpesvirus 2Viral Proteins

Identifiers

PMID19023411
PMCPMC2581436
OpenAlexW2061993905

What OpenQuestion holds

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LicenceCC BY
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.