Evidence map›Paper›PMID 24619409›Full record

ArticleThe Journal of biological chemistry2014

Differential transmembrane domain GXXXG motif pairing impacts major histocompatibility complex (MHC) class II structure.

Ann M Dixon, Lisa Drake, Kelly T Hughes, Elizabeth Sargent, Danielle Hunt, Jonathan A Harton, James R Drake

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
1.7field-weighted citation impact, top 16% 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

19 citing papers in PubMed, 33 citations in OpenAlex.

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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

7 authors at 2 institutions in 2 countries.

Ann M DixonDepartment of Chemistry, University of Warwick, Coventry CV4 7AL, United Kingdom.
Lisa DrakeCenter for Immunology and Microbial Disease, Albany Medical College, Albany, New York 12208.
Kelly T HughesCenter for Immunology and Microbial Disease, Albany Medical College, Albany, New York 12208.
Elizabeth SargentCenter for Immunology and Microbial Disease, Albany Medical College, Albany, New York 12208.
Danielle HuntCenter for Immunology and Microbial Disease, Albany Medical College, Albany, New York 12208.
Jonathan A HartonCenter for Immunology and Microbial Disease, Albany Medical College, Albany, New York 12208.
James R DrakeCenter for Immunology and Microbial Disease, Albany Medical College, Albany, New York 12208. Electronic address: drakej@mail.amc.edu.
Albany Medical Center Hospital · USUniversity of Warwick · GB

Funding

TLR2/NLR Signal Regulation of Protective Immunity to F. TularensisP01AI056320 · NIAID · ALBANY MEDICAL COLLEGE · PI METZGER, DENNIS W · 2003 to 2016
$22.9M
Establishing the Molecular Mechanisms of BCR EndocytosisR01AI065773 · NIAID · ALBANY MEDICAL COLLEGE · PI DRAKE, JAMES R · 2007 to 2011
$1.9M
MHC Class II subsets in B Lymphocyte BiologyR21AI083922 · NIAID · ALBANY MEDICAL COLLEGE · PI DRAKE, JAMES R · 2009 to 2010
$434k
ARGENTINEAN INTEGRATED PROGRAM FOR HIV/AIDS RESEARCHR03AI056321 · NIAID · ARGENTINEAN NATIONAL REFERENCE CTR/AIDS · PI SALOMON, HORACIO H · 2003 to 2004
$99k
NIAID NIH HHS AI-065773NIAID NIH HHS AI-083922NIAID NIH HHS P01 AI056320NIAID NIH HHS P01 AI-056321NIAID NIH HHS R03 AI056321NIAID NIH HHS R21 AI083922
6 · The paper itself

Abstract

Major histocompatibility complex (MHC) class II molecules exhibit conformational heterogeneity, which influences their ability to stimulate CD4 T cells and drive immune responses. Previous studies suggest a role for the transmembrane domain of the class II αβ heterodimer in determining molecular structure and function. Our previous studies identified an MHC class II conformer that is marked by the Ia.2 epitope. These Ia.2(+) class II conformers are lipid raft-associated and able to drive both tyrosine kinase signaling and efficient antigen presentation to CD4 T cells. Here, we establish that the Ia.2(+) I-A(k) conformer is formed early in the class II biosynthetic pathway and that differential pairing of highly conserved transmembrane domain GXXXG dimerization motifs is responsible for formation of Ia.2(+) versus Ia.2(-) I-A(k) class II conformers and controlling lipid raft partitioning. These findings provide a molecular explanation for the formation of two distinct MHC class II conformers that differ in their inherent ability to signal and drive robust T cell activation, providing new insight into the role of MHC class II in regulating antigen-presenting cell-T cell interactions critical to the initiation and control of multiple aspects of the immune response.

Indexed as

Amino Acid MotifsAmino Acid SequenceCell LineDimerizationEndoplasmic ReticulumHistocompatibility Antigens Class IIMolecular Sequence DataMolecular StructureSequence Homology, Amino AcidHistocompatibility Antigens Class IIAntigen PresentationLipid RaftMajor Histocompatibility Complex (MHC)Molecular ModelingProtein Conformation

Identifiers

PMID24619409
PMCPMC4002079
OpenAlexW2012401440

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.