By Bunger J.W., Li N.C. (eds.)
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2000) Proc. Natl. Acad. Sci. , 97, 571–576. Jr. (2001) Science, 294, 1346–1349. , and Carloni, P. (2008) PLoS ONE, 3, e3394 . , 158. 159. 160. 161. 162. 163. 164. 165. 166. 167. 168. 169. 170. 171.
6), that can progress from dimers to large Ub conglomerates resistant to sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE). CuII reduction by ascorbic acid or CuII chelation by ethylenediaminetetraacetic acid (EDTA) or IDA, can trigger disruption of Ub oligomers. On the other hand, when the CuII -stabilized oligomers were added to a low-polarity medium, Ub aggregation increased dramatically. 5 Cooperativity between CuII -Binding and Solvent Polarity An aqueous solution with a moderate amount (20%, v/v) of 2,2,2-triﬂuoroethanol (TFE) was used to mimic the local decrease of dielectric constant in the proximity of a membrane surface .
A major class of proteins involved in cellular Cu uptake is the copper transport (Ctr) protein family. Ctr1 is a representative member that is ubiquitously expressed. It resides predominantly in the plasma membrane and is essential for the survival of mammalian embryos and for Cu import into neurons and astrocytes . Elevated Cu stimulates rapid endocytosis and degradation of Ctr . Ctr1 contains three transmembrane helices, an N-terminal extracellular domain, and a C-terminal cytosolic domain.
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