The sun is no fun without rain : Physical environments affect how we feel about yellow across 55 countries

Across cultures, people associate colours with emotions. Here, we test the hypothesis that one driver of this cross-modal correspondence is the physical environment we live in. We focus on a prime example – the association of yellow with joy, – which conceivably arises because yellow is reminiscent of life-sustaining sunshine and pleasant weather. If so, this association should be especially strong in countries where sunny weather is a rare occurrence. We analysed yellow-joy associations of 6625 participants from 55 countries to investigate how yellow-joy associations varied geographically, climatologically, and seasonally. We assessed the distance to the equator, sunshine, precipitation, and daytime hours. Consistent with our hypotheses, participants who live further away from the equator and in rainier countries are more likely to associate yellow with joy. We did not find associations with seasonal variations. Our findings support a role for the physical environment in shaping the affective meaning of colour.Peer reviewe

Ubiquitin-specific protease 2-45 (Usp2-45) binds to epithelial Na+ channel(ENaC)ubiquitylating enzyme Nedd4-2

Regulation of the epithelial Na(+) channel (ENaC) by ubiquitylation is controlled by the activity of two counteracting enzymes, the E3 ubiquitin-protein ligase Nedd4-2 (mouse ortholog of human Nedd4L) and the ubiquitin-specific protease Usp2-45. Previously, Usp2-45 was shown to decrease ubiquitylation and to increase surface function of ENaC in Xenopus laevis oocytes, whereas the splice variant Usp2-69, which has a different N-terminal domain, was inactive toward ENaC. It is shown here that the catalytic core of Usp2 lacking the N-terminal domain has a reduced ability relative to Usp2-45 to enhance ENaC activity in Xenopus oocytes. In contrast, its catalytic activity toward the artificial substrate ubiquitin-AMC is fully maintained. The interaction of Usp2-45 with ENaC exogenously expressed in HEK293 cells was tested by coimmunoprecipitation. The data indicate that different combinations of ENaC subunits, as well as the α-ENaC cytoplasmic N-terminal but not C-terminal domain, coprecipitate with Usp2-45. This interaction is decreased but not abolished when the cytoplasmic ubiquitylation sites of ENaC are mutated. Importantly, coimmunoprecipitation in HEK293 cells and GST pull-down of purified recombinant proteins show that both the catalytic domain and the N-terminal tail of Usp2-45 physically interact with the HECT domain of Nedd4-2. Taken together, the data support the conclusion that Usp2-45 action on ENaC is promoted by various interactions, including through binding to Nedd4-2 that is suggested to position Usp2-45 favorably for ENaC deubiquitylation