RESUMEN
Due to the expansion of leadership roles in the military for women, female military personnel now face stressors equal to, and yet unique from, their male counterparts. This pilot study surveyed 73 female U.S. Army officers regarding their experiences of leadership and mental wellness within the military. A mixed-methods survey was distributed via 2 private Facebook groups for female Army officers following an anonymized convenience sampling. This anonymous, patient-centered protocol was used to protect against known stigma surrounding disclosing mental health concerns in the military. Respondents were asked a series of questions including perceived mental health status and access to behavioral health services. Most respondents reported feelings of stress related to their roles as officers (86.6%). Self-reported feelings of anxiety (83.6%) and depression (65.7%) were high. In contrast, only 30.1% had ever received a formal diagnosis of anxiety or depression by a mental health professional. Our survey confirmed a large percentage, 65.7% of respondents, reported avoiding mental/behavioral health services. Female military officers are able to recognize their feelings as symptoms of anxiety and depression; however, many take active steps to hide these symptoms from their family members and senior officers and avoid seeking professional care.
RESUMEN
In eukaryotic cells, proteins are targeted to the proteasome for degradation by polyubiquitination. These proteins bind to ubiquitin receptors, are engaged and unfolded by proteasomal ATPases, and are processively degraded. The factors determining to what extent the proteasome can successfully unfold and degrade a substrate are still poorly understood. We find that the architecture of polyubiquitin chains attached to a substrate affects the ability of the proteasome to unfold and degrade the substrate, with K48- or mixed-linkage chains leading to greater processivity than K63-linked chains. Ubiquitin-independent targeting of substrates to the proteasome gave substantially lower processivity of degradation than ubiquitin-dependent targeting. Thus, even though ubiquitin chains are removed early in degradation, during substrate engagement, remarkably they dramatically affect the later unfolding of a protein domain. Our work supports a model in which a polyubiquitin chain associated with a substrate switches the proteasome into an activated state that persists throughout the degradation process.