Educating the Colchester Community About Measles and its Prevention

Measles is a highly contagious disease with potential complications ranging from diarrhea, pneumonia, otits media, uveitis, and encephalitis. Since the introduction of the measles vaccine in 1967, incidence of measles in the United States has drastically decreased: by 1985, number of cases had fallen by 99%, by 2000, measles was declared to be eliminated from the US. Over the last decade, measles cases per year has been limited to a median of 70. In recent years however, the U.S. has seen an alarming rate of measles cases. The increasing number of measles cases per year in the U.S. highlights the need for more public awareness of the efficacy and safety of the MMR vaccine.https://scholarworks.uvm.edu/fmclerk/1058/thumbnail.jp

Obscurin and KCTD6 regulate cullin-dependent small ankyrin-1 (sAnk1.5) protein turnover.

Protein turnover through cullin-3 is tightly regulated by posttranslational modifications, the COP9 signalosome, and BTB/POZ-domain proteins that link cullin-3 to specific substrates for ubiquitylation. In this paper, we report how potassium channel tetramerization domain containing 6 (KCTD6) represents a novel substrate adaptor for cullin-3, effectively regulating protein levels of the muscle small ankyrin-1 isoform 5 (sAnk1.5). Binding of sAnk1.5 to KCTD6, and its subsequent turnover is regulated through posttranslational modification by nedd8, ubiquitin, and acetylation of C-terminal lysine residues. The presence of the sAnk1.5 binding partner obscurin, and mutation of lysine residues increased sAnk1.5 protein levels, as did knockdown of KCTD6 in cardiomyocytes. Obscurin knockout muscle displayed reduced sAnk1.5 levels and mislocalization of the sAnk1.5/KCTD6 complex. Scaffolding functions of obscurin may therefore prevent activation of the cullin-mediated protein degradation machinery and ubiquitylation of sAnk1.5 through sequestration of sAnk1.5/KCTD6 at the sarcomeric M-band, away from the Z-disk-associated cullin-3. The interaction of KCTD6 with ankyrin-1 may have implications beyond muscle for hereditary spherocytosis, as KCTD6 is also present in erythrocytes, and erythrocyte ankyrin isoforms contain its mapped minimal binding site

Circle Time Health Curriculum Designed for Pre-Schoolers

Introduction. Over 20% of low-income, Head Start eligible children are not up to date on regular healthcare exams. While many barriers exist in ensuring universal access and compliance with standard healthcare visits for young children, we sought to educate children about physician’s practices in order to engage and integrate their involvement and understanding of their well-being.https://scholarworks.uvm.edu/comphp_gallery/1197/thumbnail.jp

Identification of a mammalian-type phosphatidylglycerol- phosphate phosphatase in Rhodopirellula baltica

Cardiolipin, a glycerophospholipid with unique dimeric structure, is predominantly found in the mitochondrial membranes of eukaryotes and the membranes of bacteria. Cardiolipin interacts with protein complexes and plays pivotal roles in cellular energy metabolism, membrane dynamics, and stress responses. Recently, we identified the mitochondrial phosphatase, PTPMT1, as the enzyme responsible for catalyzing the conversion of phosphatidylglycerol-phosphate (PGP) to phosphatidylglycerol (PG), the penultimate step in the de novo biosynthesis of cardiolipin. Using phylogenomic analysis, we examined the evolutionary conservation of PTPMT1 and other cardiolipin biosynthetic enzymes. Our search identified a PTPMT1-like phosphatase in the bacterium Rhodopirellula baltica that could dephosphorylate PGP in vitro. Its expression restored cardiolipin deficiency and reversed growth impairment in Saccharomyces cerevisiae mutants lacking the yeast PGP phosphatase. When ectopically expressed, the bacterial PGP phosphatase localized to the mitochondria of yeast and mammalian cells. This suggests that the N-terminus of the R. baltica ortholog can be used as a mitochondrial targeting sequence in eukaryotes. Together, our study demonstrates the conservation of function between bacterial and mammalian PTPMT1 orthologs and establishes an approach to investigate the function of other cardiolipin enzymes in parasitic organism

Obscurin and KCTD6 regulate cullin-dependent small ankyrin-1 (sAnk1.5) protein turnover

Protein turnover through cullin-3 is tightly regulated by posttranslational modifications, the COP9 signalosome, and BTB/POZ-domain proteins that link cullin-3 to specific substrates for ubiquitylation. In this paper, we report how potassium channel tetramerization domain containing 6 (KCTD6) represents a novel substrate adaptor for cullin-3, effectively regulating protein levels of the muscle small ankyrin-1 isoform 5 (sAnk1.5). Binding of sAnk1.5 to KCTD6, and its subsequent turnover is regulated through posttranslational modification by nedd8, ubiquitin, and acetylation of C-terminal lysine residues. The presence of the sAnk1.5 binding partner obscurin, and mutation of lysine residues increased sAnk1.5 protein levels, as did knockdown of KCTD6 in cardiomyocytes. Obscurin knockout muscle displayed reduced sAnk1.5 levels and mislocalization of the sAnk1.5/KCTD6 complex. Scaffolding functions of obscurin may therefore prevent activation of the cullin-mediated protein degradation machinery and ubiquitylation of sAnk1.5 through sequestration of sAnk1.5/KCTD6 at the sarcomeric M-band, away from the Z-disk–associated cullin-3. The interaction of KCTD6 with ankyrin-1 may have implications beyond muscle for hereditary spherocytosis, as KCTD6 is also present in erythrocytes, and erythrocyte ankyrin isoforms contain its mapped minimal binding site