Do sexist mothers change more diapers? Ambivalent sexism, maternal gatekeeping and the division of childcare

This study examined the role of ambivalent sexist ideologies in the division of childcare responsibilities. It proposed maternal gatekeeping as a mediator through which hostile sexist attitudes toward men and women facilitate gendered division of childcare. A sample of 207 mothers with at least one child aged 6 years or younger completed extensive questionnaires. As hypothesized, the mother’s hostile sexist attitudes toward men and women were positively related to maternal gatekeeping tendencies. Gatekeeping, in turn, was related to the mother’s greater time investment in childcare and greater share of childcare tasks relative to the father. Finally, hostile sexist attitudes toward men and women had an indirect effect on the mother’s hours of care and relative share of childcare tasks, mediated though maternal gatekeeping. The findings underscore the importance of investigating the mechanisms through which sexist ideologies are translated into daily behaviors that help maintain a gendered social structure. They may be utilized to inform parenting interventions aimed at increasing collaborative family work and fathers’ participation

NR3C2 (nuclear receptor subfamily 3, group C, member 2)

Review on NR3C2 (nuclear receptor subfamily 3, group C, member 2), with data on DNA, on the protein encoded, and where the gene is implicated

Phosphorylation of Pirh2 by Calmodulin-dependent kinase II impairs its ability to ubiquitinate p53

Although the recently identified Pirh2 protein is known as a p53-induced ubiquitin-protein E3 ligase, which negatively regulates p53, the detailed mechanism underlying the regulation of Pirh2 remains largely unknown. Here, we demonstrate that while Pirh2 is mostly detected in the phosphorylated form in normal tissues, it is predominantly present in the unphosphorylated form in majority of tumor cell lines and tissues examined. Phosphorylated Pirh2 is far more unstable than its unphosphorylated form. We further identified that Calmodulin-dependent kinase II (CaMK II) phosphorylates Pirh2 on residues Thr-154 and Ser-155. Phosphorylation of Pirh2 appears to be regulated through cell cycle-dependent mechanism. CaMK II-mediated Pirh2 phosphorylation abrogates its E3 ligase activity toward p53. Together, our data suggest that phosphorylation of Pirh2 may act as a fine-tuning to maintain the balance of p53-Pirh2 autoregulatory feedback loop, which facilitates the tight regulation of p53 stability and tumor suppression