ABSTRACT
Diabetes disproportionately affects racial and ethnic minorities, rural, and impoverished populations. This case study describes the program components and key lessons learned from implementing Vivir Mejor! (Live Better!), a diabetes prevention and management program tailored for the rural, Mexican American population. The program used workforce innovations and multisector partnerships to engage and activate a rural, mostly Hispanic population. Community health worker (CHW) roles were designed to reach and support distinct populations. Promotoras focused exclusively on health education and patient navigators individually coached patients with chronic disease management issues for the high-risk patient population. To extend diabetes health education to the broader community in Santa Cruz County, promotoras trained lay leaders to become peer educators. Multisector partnerships allowed the program to offer health and social services around diabetes care. The partners also supported provider engagement through continuing education workshops and digital story screening to encourage referrals to the program. Multisector partnerships, including partnering with critical access hospitals, for diabetes management and prevention, as well as using different types of CHWs to implement programs that target high- and low-risk populations are innovative and valuable components of the Vivir Mejor!
Subject(s)
Community Health Workers/organization & administration , Diabetes Mellitus/prevention & control , Health Education/organization & administration , Mexican Americans , Rural Population , Community Health Workers/education , Diabetes Mellitus/ethnology , Diabetes Mellitus/therapy , Health Promotion , Healthy Lifestyle , Humans , Interinstitutional Relations , Self-ManagementABSTRACT
The ubiquitin-specific protease, USP7, has key roles in the p53 pathway whereby it stabilizes both p53 and MDM2. We show that the N-terminal domain of USP7 binds two closely spaced 4-residue sites in both p53 and MDM2, falling between p53 residues 359-367 and MDM2 residues 147-159. Cocrystal structures with USP7 were determined for both p53 peptides and for one MDM2 peptide. These peptides bind the same surface of USP7 as Epstein-Barr nuclear antigen-1, explaining the competitive nature of the interactions. The structures and mutagenesis data indicate a preference for a P/AXXS motif in peptides that bind USP7. Contacts made by serine are identical and crucial for all peptides, and Trp165 in the peptide-binding pocket of USP7 is also crucial. These results help to elucidate the mechanism of substrate recognition by USP7 and the regulation of the p53 pathway.
