Ensemble coding of color and luminance contrast

Ensemble coding has been demonstrated for many attributes including color, but the metrics on which this coding is based remain uncertain. We examined ensemble percepts for stimulus sets that varied in chromatic contrast between complementary hues, or that varied in luminance contrast between increments and decrements, in both cases focusing on the ensemble percepts for the neutral gray stimulus defining the category boundary. Each ensemble was composed of 16 circles with four contrast levels. Observers saw the display for 0.5 s and then judged whether a target contrast was a member of the set. False alarms were high for intermediate contrasts (within the range of the ensemble) and fell for higher or lower values. However, for ensembles with complementary hues, gray was less likely to be reported as a member, even when it represented the mean chromaticity of the set. When the settings were repeated for luminance contrast, false alarms for gray were higher and fell off more gradually for out-of-range contrasts. This difference implies that opposite luminance polarities represent a more continuous perceptual dimension than opponent-color variations, and that “gray” is a stronger category boundary for chromatic than luminance contrasts. For color, our results suggest that ensemble percepts reflect pooling within rather than between large hue differences, perhaps because the visual system represents hue differences more like qualitatively different categories than like quantitative differences within an underlying color “space.” The differences for luminance and color suggest more generally that ensemble coding for different visual attributes might depend on different processes that in turn depend on the format of the visual representation

Distinct Prion Domain Sequences Ensure Efficient Amyloid Propagation by Promoting Chaperone Binding or Processing <i>In Vivo</i>

<div><p>Prions are a group of proteins that can adopt a spectrum of metastable conformations <i>in vivo</i>. These alternative states change protein function and are self-replicating and transmissible, creating protein-based elements of inheritance and infectivity. Prion conformational flexibility is encoded in the amino acid composition and sequence of the protein, which dictate its ability not only to form an ordered aggregate known as amyloid but also to maintain and transmit this structure <i>in vivo</i>. But, while we can effectively predict amyloid propensity <i>in vitro</i>, the mechanism by which sequence elements promote prion propagation <i>in vivo</i> remains unclear. In yeast, propagation of the [<i>PSI</i>^<i>+</i>] prion, the amyloid form of the Sup35 protein, has been linked to an oligopeptide repeat region of the protein. Here, we demonstrate that this region is composed of separable functional elements, the repeats themselves and a repeat proximal region, which are both required for efficient prion propagation. Changes in the numbers of these elements do not alter the physical properties of Sup35 amyloid, but their presence promotes amyloid fragmentation, and therefore maintenance, by molecular chaperones. Rather than acting redundantly, our observations suggest that these sequence elements make complementary contributions to prion propagation, with the repeat proximal region promoting chaperone binding to and the repeats promoting chaperone processing of Sup35 amyloid.</p></div