Objective: Simpatía, a term that captures the tendency to prefer and create social interactions characterized by warmth and emotional positivity while also avoiding conflict and/or overt negativity, is a cultural factor relevant to Latinos. The goal of this article was to develop a scale that measures this cultural value. Method: A self-report scale measure of simpatía was developed and administered to a combined sample of Latinos (N ϭ 296) drawn from 3 larger studies. The scale's factor structure was explored, and its internal consistency and validity were tested. Results: Exploratory factor analysis supported an 18-item scale and indicated 2 factors: simpatía-related positivity/warmth and simpatíarelated negativity/conflict avoidance. Cronbach's alphas for the overall scale and subscales showed internal consistency. Validity analyses revealed that across subscales, simpatía was positively associated with positive emotion expressivity and dispositional positive emotion. The simpatía-related positivity/ warmth subscale was also positively associated with an orientation toward Latino culture. Conclusions: The Simpatía Scale, which captures dual aspects of simpatía that emphasize the positive and avoid the negative, provides a new tool for advancing the study of Latino culture. Public Significance StatementEthnicity is still too often used as a proxy for culture and, as such, measures are needed to help researchers avoid this limitation. To address this need, we developed and validated the "Simpatía Scale" to measure simpatía, a Latino cultural value that emphasizes warmth/positive emotion expression and avoiding conflict and negativity.

PGAM5 is a mitochondrial protein phosphatase whose genetic ablation in mice results in mitochondria-related disorders, including neurodegeneration. Functions of PGAM5 include regulation of mitophagy, cell death, metabolism and aging. However, mechanisms regulating PGAM5 activation and signaling are poorly understood. Using electron cryo-microscopy, we show that PGAM5 forms dodecamers in solution. We also present a crystal structure of PGAM5 that reveals the determinants of dodecamer formation. Furthermore, we observe PGAM5 dodecamer assembly into filaments both in vitro and in cells. We find that PGAM5 oligomerization into a dodecamer is not only essential for catalytic activation, but this form also plays a structural role on mitochondrial membranes, which is independent of phosphatase activity. Together, these findings suggest that modulation of the oligomerization of PGAM5 may be a regulatory switch of potential therapeutic interest.

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