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1.
Rand Health Q ; 11(2): 1, 2024 Mar.
Article in English | MEDLINE | ID: mdl-38601716

ABSTRACT

Like the United States as a whole, Virginia faces a significant shortage of health care workers in nursing, primary care, and behavioral health. If current trends persist, these shortages will increase across Virginia. The authors of this study identify interventions that can help the Virginia Health Workforce Development Authority (VHWDA) address these health care workforce shortages. To accomplish this goal, they applied an analytic framework to existing or potential interventions for retaining, recruiting, and improving the structural efficiency of the nursing, primary care, and behavioral health workforces in Virginia. In this study, they highlight which interventions VHWDA should prioritize based on its desired outcomes and policy goals.

2.
Rand Health Q ; 10(2): 1, 2023 May.
Article in English | MEDLINE | ID: mdl-37200824

ABSTRACT

Many of the ethnic and racial workforce inequities in the United States are present in health care systems. Low representation of African American/Black individuals in the health care system workforce can be traced to a history of exclusionary practices that leave such individuals less likely to pursue health careers. Past research found that low representation is driven by inequities in health, education, and employment that are a result of structural racism. Pathways programs have been identified as one of the methods to increase recruitment, retention, and promotion in health-related career fields for African American/Black individuals. As prior research has shown, these programs recruit and support the graduation of students from underrepresented communities at all educational stages to increase their representation in specific fields. This article describes the development of key factors in framework design for the Health System-Community Pathways Program (HCPP), which aims to increase representation of African American/Black communities in the health care system workforce and improve the quality of their experience in pursuing careers in these fields. The HCPP framework of key factors is informed by an environmental scan, interviews and focus groups, and an expert discussion panel session. The article's authors come from diverse backgrounds; the team included African American/Black physicians and members of other historically marginalized communities. The qualitative research drew insights from diverse African American/Black community stakeholders; the study was reviewed by many stakeholders to ensure that the design of the research and the end product maximally benefits the community on which it focuses.

3.
Biochem Biophys Res Commun ; 482(4): 1341-1345, 2017 Jan 22.
Article in English | MEDLINE | ID: mdl-27939891

ABSTRACT

Ubiquitination is a key regulatory mechanism that affects numerous cellular processes. This modification is reversible. Deubiquitinating enzymes (DUBs) remove the ubiquitin tag from modified proteins. DUB Doa4 is involved in deubiquitination of conjugates at the late endosome/pre vacuolar compartment. A genetic screen led to isolation of seven extragenic suppressors of the doa4 phenotypic abnormalities. Remarkably, cloned Doa4-independent degradation (DID) genes encode the class E vacuolar protein-sorting factors involved in membrane protein trafficking. Here we provide evidence that inactivation of Vid27 (vacuolar import and degradation) prevents suppression of the doa4 phenotype by did3 mutation. Vid27 is a cytoplasmic protein essential for delivery of fructose-1,6-bisphosphatase into VID vesicles. Thus, our data revealed another connection between Doa4 and vacuolar protein sorting.


Subject(s)
Mutation , Saccharomyces cerevisiae Proteins/genetics , Saccharomyces cerevisiae/genetics , Vesicular Transport Proteins/biosynthesis , Endopeptidases/genetics , Endosomal Sorting Complexes Required for Transport/genetics , Endosomal Sorting Complexes Required for Transport/metabolism , Fructose-Bisphosphatase/metabolism , Genes, Reporter , Green Fluorescent Proteins/metabolism , Mutagenesis , Phenotype , Protein Transport , Saccharomyces cerevisiae Proteins/biosynthesis , Saccharomyces cerevisiae Proteins/metabolism , Ubiquitin Thiolesterase/genetics , Ubiquitination , Vacuoles/metabolism
4.
Biochem Biophys Res Commun ; 467(3): 570-6, 2015 Nov 20.
Article in English | MEDLINE | ID: mdl-26427873

ABSTRACT

Ubiquitination is involved in numerous cellular regulatory mechanisms including the cell cycle, signal transduction and quality control. Ubiquitin modifies proteins by consecutive actions of ubiquitin-activating/conjugating enzymes. Attachment of ubiquitin is reversible. Deubiquitinating enzymes are responsible for removal of ubiquitin from ubiquitin-protein conjugates. Genome of the yeast Saccharomyces cerevisiae encodes structurally related but functionally distinct enzymes - Doa4 and Ubp5. Doa4 is involved in general ubiquitin-dependent proteolysis and is responsible for deubiquitination of ubiquitin-protein conjugates at the cytoplasmic face of the late endosome. The N-terminal domain targets the enzyme to the endosome membrane after ESCRT-III complex has formed there. By contrast, corresponding region of homologous Ubp5 is critical for its bud neck localization in dividing cells. Conceivably, Ubp5 plays an essential role in cytokinesis. Here we show that Doa4 physically interacts with the ESCRT-III component Snf7 and preferentially cleaves Lys63-linked ubiquitin oligomers involved in membrane protein trafficking. We also demonstrate that the unstable regulator of cytokinesis Hof1 accumulates in proteasomal mutants and is required for cellular localization of Ubp5.


Subject(s)
Endopeptidases/metabolism , Endosomal Sorting Complexes Required for Transport/metabolism , Saccharomyces cerevisiae Proteins/metabolism , Ubiquitin Thiolesterase/metabolism , Endopeptidases/chemistry , Endosomal Sorting Complexes Required for Transport/chemistry , Endosomes/metabolism , Protein Binding , Saccharomyces cerevisiae/metabolism , Saccharomyces cerevisiae Proteins/chemistry , Ubiquitin Thiolesterase/chemistry , Ubiquitination
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