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Social chatbots are aimed at building emotional bonds with users, and thus it is particularly important to design these technologies so as to elicit positive perceptions from users. In the current study, we investigate the impacts that transparent explanations of chatbots’ mechanisms have on users’ perceptions of the chatbots. A total of 914 participants were recruited from Amazon Mechanical Turk. They were randomly assigned to observe conversations between a hypothetical chatbot and a user in one of the two-by-two experimental conditions: whether the participants received an explanation about how the chatbot was trained and whether the chatbot was framed as an intelligent entity or a machine. A fifth group, who believed they were observing interactions between two humans, served as a control. Analyses of participants’ responses to the postobservation survey indicated that transparency positively affected perceptions of social chatbots by leading users to (1) find the chatbot less creepy, (2) feel greater affinity to the chatbot, and (3) perceive the chatbot as more socially intelligent, though these effects were small. Moreover, transparency appeared to have a larger effect on increasing the perceived social intelligence among participants with lower prior AI knowledge. These findings have implications for the design of future social chatbots and support the addition of transparency and explanation for chatbot users.

Liquid–liquid phase separation (LLPS) underlies diverse biological processes. Because most LLPS studies were performed in vitro using recombinant proteins or in cells that overexpress protein, the physiological relevance of LLPS for endogenous protein is often unclear. PERIOD, the intrinsically disordered domain-rich proteins, are central mammalian circadian clock components and interact with other clock proteins in the core circadian negative feedback loop. Different core clock proteins were previously shown to form large complexes. Circadian clock studies often rely on experiments that overexpress clock proteins. Here, we show that when Per2 transgene was stably expressed in cells, PER2 protein formed nuclear phosphorylation-dependent slow-moving LLPS condensates that recruited other clock proteins. Super-resolution microscopy of endogenous PER2, however, revealed formation of circadian-controlled, rapidly diffusing nuclear microbodies that were resistant to protein concentration changes, hexanediol treatment, and loss of phosphorylation, indicating that they are distinct from the LLPS condensates caused by protein overexpression. Surprisingly, only a small fraction of endogenous PER2 microbodies transiently interact with endogenous BMAL1 and CRY1, a conclusion that was confirmed in cells and in mice tissues, suggesting an enzyme-like mechanism in the circadian negative feedback process. Together, these results demonstrate that the dynamic interactions of core clock proteins are a key feature of mammalian circadian clock mechanism and the importance of examining endogenous proteins in LLPS and circadian clock studies.