Measuring the closeness of relationships: a comprehensive evaluation of the 'Inclusion of the Other in the Self' scale

Understanding the nature and influence of social relationships is of increasing interest to behavioral economists, and behavioral scientists more generally. In turn, this creates a need for tractable, and reliable, tools for measuring fundamental aspects of social relationships. We provide a comprehensive evaluation of the 'Inclusion of the Other in the Self' (IOS) Scale, a handy pictorial tool for measuring the subjectively perceived closeness of a relationship. The tool is highly portable, very easy for subjects to understand and takes less than 1 minute to administer. Across our three online studies with a diverse adult population (n=772) we show that six different scales designed to measure relationship closeness are all highly significantly positively correlated with the IOS Scale. We then conduct a Principal Component Analysis to construct an Index of Relationship Closeness and find that it correlates very strongly (ρ=.85) with the IOS Scale. We conclude that the IOS Scale is a psychologically meaningful and highly reliable measure of the subjective closeness of relationships

TBP Binding-Induced Folding of the Glucocorticoid Receptor AF1 Domain Facilitates Its Interaction with Steroid Receptor Coactivator-1

The precise mechanism by which glucocorticoid receptor (GR) regulates the transcription of its target genes is largely unknown. This is, in part, due to the lack of structural and functional information about GR's N-terminal activation function domain, AF1. Like many steroid hormone receptors (SHRs), the GR AF1 exists in an intrinsically disordered (ID) conformation or an ensemble of conformers that collectively appears to be unstructured. The GR AF1 is known to recruit several coregulatory proteins, including those from the basal transcriptional machinery, e.g., TATA box binding protein (TBP) that forms the basis for the multiprotein transcription initiation complex. However, the precise mechanism of this process is unknown. We have earlier shown that conditional folding of the GR AF1 is the key for its interactions with critical coactivator proteins. We hypothesize that binding of TBP to AF1 results in the structural rearrangement of the ID AF1 domain such that its surfaces become easily accessible for interaction with other coactivators. To test this hypothesis, we determined whether TBP binding-induced structure formation in the GR AF1 facilitates its interaction with steroid receptor coactivator-1 (SRC-1), a critical coactivator that is important for GR-mediated transcriptional activity. Our data show that stoichiometric binding of TBP induces significantly higher helical content at the expense of random coil configuration in the GR AF1. Further, we found that this induced AF1 conformation facilitates its interaction with SRC-1, and subsequent AF1-mediated transcriptional activity. Our results may provide a potential mechanism through which GR and by large other SHRs may regulate the expression of the GR-target genes