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The implicit discount rate (IDR) is a decisive factor in household investment decisions, and its modification could promote investment in energy-saving products. However, the discussion on households' IDR in developing countries is limited. In this regard, the current study aims to provide a detailed review of the IDR across various investment decisions, factors affecting its value, and policy instruments that can influence its value. The study finds that the IDR value tends to be considerably higher than market interest rates. Information and behavioural failures lead to a high IDR and under-investment in energy efficiency, which may be addressed through energy labels. However, the effectiveness of energy labels in addressing barriers and making energy-efficiency information visible to households depends on their visual presentation, time frame (annual or lifetime), units of measurement (physical or monetary), and the content of the information. The review has relevance for policymaking aimed at increasing the adoption of energy-efficient options that reduce household carbon footprints and, in turn, contribute towards realizing the net-zero emissions target. [ABSTRACT FROM AUTHOR]

Abstract: Free fatty acid receptor 4 (FFA4), previously known as GPR120, is a G protein-coupled receptor that promotes numerous anti-inflammatory and antidiabetic effects upon its agonism by long chained unsaturated fatty acids. We have previously demonstrated that agonism of FFA4 with docosahexaenoic acid (DHA) and alpha-linoleic acid (ALA) facilitates rapid and transient phosphorylation of FFA4 expressed ectopically on the surface of HEK293 cells. However, the precise mechanisms that promote FFA4 phosphorylation remain elusive. In the current study, we examined the mechanisms behind both heterologous and homologous phosphorylation of FFA4 and set out to identify the foci of FFA4 phosphorylation. Our results demonstrate that basal and heterologous phosphorylation of FFA4 are mediated by protein kinase C (PKC), while G protein-coupled receptor kinase 6 (GRK6) plays the predominant role in DHA-mediated phosphorylation of FFA4. Furthermore, we identify Thr347, Ser350, and Ser357 in the C-terminal tail as major sites of FFA4 phosphorylation. Concurrent mutation of these three sites leads to a FFA4 receptor that seemingly affects Gαq/11 signaling in a positive manner as demonstrated by heightened intracellular Ca2+ responses following agonism with DHA. Importantly, this phosphodefective FFA4 mutant lacked the ability to promote β-arrestin-2 recruitment to the cell membrane. Since many of the functionally beneficial physiological effects of FFA4 are noted to be β-arrestin mediated, these findings could provide insight into the structural requirements for FFA4 function. [Copyright &y& Elsevier]