A5063026067- Genetics, Aging, and Longevity in Model Organisms
- 14-3-3 protein interactions
- Ubiquitin and proteasome pathways
- Endoplasmic Reticulum Stress and Disease
- Protein Tyrosine Phosphatases
- Heat shock proteins research
- Cellular Mechanics and Interactions
- Protein Kinase Regulation and GTPase Signaling
University of Wisconsin–Milwaukee
2022-2024
Raf protein kinases act as Ras-GTP sensing components of the ERK signal transduction pathway in animal cells, influencing cell proliferation, differentiation, and survival. In humans, somatic germline mutations genes
Signaling by the kinase cascade composed of Raf, MEK, and ERK is critical for animal development often inappropriately activated in human malignancies. We sought to identify factors that control signaling mediated Caenorhabditis elegans Raf ortholog LIN-45. A genetic screen showed degradation LIN-45 required E3/E4 ubiquitin ligase UFD-2. Both UFD-2 its partner, ATP-dependent segregase CDC-48, were developmental regulation protein abundance. acted same pathway as E3 SCFSEL-10 decrease...
Abstract Raf protein kinases act as Ras-GTP sensing components of the ERK signal transduction pathway in animal cells, influencing cell proliferation, differentiation, and survival. In humans, somatic germline mutations genes BRAF RAF1 are associated with malignancies developmental disorders. Recent studies shed light on structure activated Raf, a heterotetramer consisting 14-3-3 dimers, raised possibility that C-terminal distal tail segment (DTS) regulates activation. We investigated role...
Abstract Signaling by the kinase cascade comprised of Raf, MEK, and ERK is critical for animal development; moreover, its inappropriate activation commonly found in human malignancies. In a genetic screen factors that control signaling Caenorhabditis elegans Raf ortholog LIN-45, we it negatively regulated E3/E4 ubiquitin ligase UFD-2. Both UFD-2 partner, ATP-dependent unfoldase CDC-48, were required degradation LIN-45 protein. Our structure-function studies showed disruption domains mediate...