The role of supramolecular protein complexes and membrane potential in transmembrane signaling processes of lymphocytes

Open conformers: the hidden face of MHC-I molecules

“…MHC-I homodimer formation and clustering is thought to strengthen antigen recognition by CD8 + T cells, most probably through the formation of a more stable immunological synapse [49,79], suggesting that membrane reorganization of MHC-I molecules on antigen-presenting cells can modulate the sensitivity of T cell recognition [80]. Supporting this view is a recent study showing that HLA-G homodimers enhance the efficiency of the signaling following interaction with leukocyte immunoglobulin-like receptors LILRB1 and LILRB2, which are members of the family of inhibitory NK receptors [81].…”

A biophysical approach to IL-2 and IL-15 receptor function: Localization, conformation and interactions

“…Protein-protein interactions can influence the efficiency of receptor signaling [103], and may be a key element in the diverging signaling pathways of IL-2 and IL-15 pathways. Therefore it is an interesting question, what is the direct molecular environment of these receptors.…”

Single-spanning transmembrane domains in cell growth and cell-cell interactions

“…But, it may also play a role in signaling across cell membranes by associating two similar or different proteins in an active (or inactive) dimer or by creating larger oligomeric structures. 17 Many examples of such membrane complexes are known, e.g., the photosynthetic apparatus, 18 ATPases, 19 virus assembly machinery, 20 immune signalling, [21][22][23] G protein-coupled receptors, 24,25 etc. It is becoming increasingly clear that protein interactions, both transient and stable, are far more extensive than originally appreciated.…”