NDLI: Evidence for role of transmembrane helix–helix interactions in the assembly of the Class II major histocompatibility complex

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Molecular BioSystems Vol - 6 Issue - 8

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Evidence for role of transmembrane helix–helix interactions in the assembly of the Class II major histocompatibility complex

Content Provider	Royal Society of Chemistry (RSC)
Author	King, Gavin Dixon, Ann M.
Copyright Year	2010
Abstract	The Major Histocompatibility Complex Class II (Class II MHC) and invariant chain (Ii) proteins are key initiators of an immune response to invading pathogens. Following biosynthesis, three MHCα/β hetero-dimers associate with an Ii homotrimer to form a nine-chain protein complex. Only as part of this complex are the MHC molecules exported to the cell surface to trigger an immune response. Previous reports implicate the transmembrane (TM) domains of all three proteins in correct assembly, ligand binding and function of Class II MHC. Building on our previous work that revealed the Ii TM domain may contribute significantly to correct assembly of the full-length protein, we have used a variety of genetic, biophysical and computational methods to investigate the role of the TM domains in stabilizing MHCα/β heterodimers. Using the in vivo GALLEX assay, we find that the TM domains of both proteins form strong homo- and hetero-oligomers in natural membranes that are stabilized by GXXXG motifs within the sequence. Förster resonance energy transfer (FRET) measurements, using fluorescently-tagged peptides derived from the TM domains of each protein, were then employed to confirm the presence of TM helix–helix hetero-interactions in detergent micelles, as well as the stoichiometry of these interactions. Our results are summarized in a revised model of Class II MHC–Ii complex formation that illustrates key protein–protein contacts. This work provides the first evidence that the TM domains of the Class II MHC molecules are capable of significant protein–protein interactions that may help to stabilize or even initiate formation of the MHC–Ii complex.
Starting Page	1650
Ending Page	1661
Page Count	12
File Format	HTM / HTML PDF
ISSN	1742206X
Volume Number	6
Issue Number	9
Journal	Molecular BioSystems
DOI	10.1039/c002241a
Language	English
Publisher	Royal Society of Chemistry
Access Restriction	Open
Subject Keyword	CD74 Förster resonance energy transfer Stoichiometry GALLEX Major histocompatibility complex Ligand Protease Protein
Content Type	Text
Resource Type	Article
Subject	Molecular Biology Biotechnology

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Major histocompatibility complex class I protein conformation altered by transmembrane potential changes

Role of membrane environment and membrane-spanning protein regions in assembly and function of the Class II Major Histocompatibility complex

Differential Transmembrane Domain GXXXG Motif Pairing Impacts Major Histocompatibility Complex (MHC) Class II Structure

SCIMP, a Transmembrane Adaptor Protein Involved in Major Histocompatibility Complex Class II Signaling ▿ †

Role of the major histocompatibility complex class II transmembrane region in antigen presentation and intracellular trafficking

Human immunodeficiency virus type 1 Vpu protein interacts with CD74 and modulates major histocompatibility complex class II presentation.

Invariant chain transmembrane domain trimerization: a step in mhc class ii assembly† (2005).

Complex architecture of major histocompatibility complex class II promoters: reiterated motifs and conserved protein-protein interactions.

SCIMP, a transmembrane adaptor protein involved in major histocompatibility complex class II signaling.

Evidence for role of transmembrane helix–helix interactions in the assembly of the Class II major histocompatibility complex

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Major histocompatibility complex class I protein conformation altered by transmembrane potential changes

Role of membrane environment and membrane-spanning protein regions in assembly and function of the Class II Major Histocompatibility complex

Differential Transmembrane Domain GXXXG Motif Pairing Impacts Major Histocompatibility Complex (MHC) Class II Structure

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Evidence for role of transmembrane helix–helix interactions in the assembly of the Class II major histocompatibility complex