When I took a look at Hemmi, H. et al. ‘s paper several years ago, I almost automatically assumed Toll-like receptor 9 (TLR9) to be monomeric and span the cell membrane like this figure. However, I later noticed its dimeric model (see also Lichtman, M.A. et al. eds. Williams Hematology 7th ed. McGraw-Hill Medical 2005, p233.) and subcellular localization study which indicates that it is located to the endoplasmic reticulum (ER) of dendritic cells or macrophages. Furthermore, a more recent study shows that it can be localized also on the cell surface of non-immune cells.
So I wish to raise the following three questions:
1. Can we determine the stoichiometry of full-length human TLR9 using AFM in solution?
2. Is the stoichiometry tissue-dependent or not?
I have just noticed a paper demonstrating expression of human TLR9 in prostate cancer cells.
(for its expression in other tissues, see here.)
Is dimeric model predominant?
For a recent application of AFM in dendritic cell research, see here.
Are all TLRs dimeric?
Is monomeric model of TLR9 still viable?
Again, are all TLRs dimeric?
I have been unaware of TLR expression on airway epithelial cells.
Does human UNC93B(1) bind to human TLR9?
Is UNC93B itself a motor protein?
Again, is UNC93B itself a motor protein?
I have just noticed this paper.
Addendum tertium decimum:
Are all TLRs monomeric?
Addendum quartum decimum:
Will the author(s) of this paper employ yeast two-hybrid method?
Addendum quintum decimum:
Addendum sextum decimum: