@article {65286,
	title = {Structure and assembly of calcium homeostasis modulator proteins.},
	journal = {Nature Structural and Molecular Biology},
	volume = {27},
	year = {2020},
	month = {2020 Jan 27},
	pages = {150-9},
	abstract = {<p>The biological membranes of many cell types contain large-pore channels through which a wide variety of ions and metabolites permeate. Examples include connexin, innexin and pannexin, which form gap junctions and/or bona fide cell surface channels. The most recently identified large-pore channels are the calcium homeostasis modulators (CALHMs), through which ions and ATP permeate in a voltage-dependent manner to control neuronal excitability, taste signaling and pathologies of depression and Alzheimer{\textquoteright}s disease. Despite such critical biological roles, the structures and patterns of their oligomeric assembly remain unclear. Here, we reveal the structures of two CALHMs, chicken CALHM1 and human CALHM2, by single-particle cryo-electron microscopy (cryo-EM), which show novel assembly of the four transmembrane helices into channels of octamers and undecamers, respectively. Furthermore, molecular dynamics simulations suggest that lipids can favorably assemble into a bilayer within the larger CALHM2 pore, but not within CALHM1, demonstrating the potential correlation between pore size, lipid accommodation and channel activity.</p>
},
	issn = {1545-9985},
	doi = {10.1038/s41594-019-0369-9},
	author = {Syrjanen, Johanna L and Michalski, Kevin and Chou, Tsung-Han and Grant, Timothy and Rao, Shanlin and Simorowski, Noriko and Tucker, Stephen J and Grigorieff, Nikolaus and Furukawa, Hiro}
}
