Connecting groups and behaviours: A network analysis of identity-infused behaviours.

Research in the social identity tradition acknowledges the multiplicity of our identities and the implications that identity compatibility has for our health and well-being. However, current measures of multiple group membership have not yet captured the richness and complexity of our social identity networks at the wider sample level, and data regarding the different behaviours typically associated with different group memberships are scarce. Adopting a network approach, we explore the co-occurrence of different group memberships within an individual (identity-by-identity network), the behaviours that are shared among identities (behaviour-by-identity network), and whether identities that are shared also share common behaviours (identity-by-behaviour network). An online survey asked participants (N = 286) to list the groups they are part of, as well as the behaviours viewed to be typical of group members. The networks identified several identities and behaviours to significantly co-occur at a rate both higher and lower than chance. Networks were found to be low in modularity; there was no evidence of clustering within the data. Permutation analyses demonstrated the overall structure of the networks to be significantly different than expected by chance. The co-occurrences identified serve as a meaningful resource for those conducting research into identities, group norms and their associated behaviours.

An inverse agonist of orphan receptor GPR61 acts by a G protein-competitive allosteric mechanism.

GPR61 is an orphan GPCR related to biogenic amine receptors. Its association with phenotypes relating to appetite makes it of interest as a druggable target to treat disorders of metabolism and body weight, such as obesity and cachexia. To date, the lack of structural information or a known biological ligand or tool compound has hindered comprehensive efforts to study GPR61 structure and function. Here, we report a structural characterization of GPR61, in both its active-like complex with heterotrimeric G protein and in its inactive state. Moreover, we report the discovery of a potent and selective small-molecule inverse agonist against GPR61 and structural elucidation of its allosteric binding site and mode of action. These findings offer mechanistic insights into an orphan GPCR while providing both a structural framework and tool compound to support further studies of GPR61 function and modulation.