A5032167940- 14-3-3 protein interactions
- Protein Tyrosine Phosphatases
- Galectins and Cancer Biology
- Ubiquitin and proteasome pathways
- Neurological diseases and metabolism
- Parkinson's Disease Mechanisms and Treatments
- Cancer, Hypoxia, and Metabolism
- ATP Synthase and ATPases Research
- Cancer-related Molecular Pathways
- RNA regulation and disease
- Mitochondrial Function and Pathology
- Microbial metabolism and enzyme function
- Steroid Chemistry and Biochemistry
Brigham Young University
2021-2023
Stanford University
2022-2023
Dysregulated iron or Ca
PTOV1 is an oncogenic protein, initially identified in prostate cancer, that promotes proliferation, cell motility, and invasiveness. However, the mechanisms regulate remain unclear. Here, we identify 14-3-3 as a interactor show high levels of expression, like PTOV1, correlate with cancer progression. We discover SGK2-mediated phosphorylation at S36, which required for binding. Disruption PTOV1-14-3-3 interaction results accumulation nucleus proteasome-dependent reduction protein levels....
Summary Dysregulated iron or Ca 2+ homeostasis has been reported in Parkinson’s disease (PD) models. Here we discover a connection between these two metals at the mitochondria. Elevation of levels causes inward mitochondrial overflow, through an interaction Fe with Mitochondrial Calcium Uniporter. In PD neurons, accumulation-triggered influx across surface leads to spatially confined elevation outer membrane, which is subsequently sensed by Miro1, -binding protein. A Miro1 blood test...
Supplementary Data from SGK2, 14-3-3, and HUWE1 Cooperate to Control the Localization, Stability, Function of Oncoprotein PTOV1
Supplementary Data from SGK2, 14-3-3, and HUWE1 Cooperate to Control the Localization, Stability, Function of Oncoprotein PTOV1
Supplementary Data from SGK2, 14-3-3, and HUWE1 Cooperate to Control the Localization, Stability, Function of Oncoprotein PTOV1
<div>Abstract<p>PTOV1 is an oncogenic protein, initially identified in prostate cancer, that promotes proliferation, cell motility, and invasiveness. However, the mechanisms regulate PTOV1 remain unclear. Here, we identify 14-3-3 as a interactor show high levels of expression, like PTOV1, correlate with cancer progression. We discover SGK2-mediated phosphorylation at S36, which required for binding. Disruption PTOV1–14–3-3 interaction results accumulation nucleus...
Supplementary Data from SGK2, 14-3-3, and HUWE1 Cooperate to Control the Localization, Stability, Function of Oncoprotein PTOV1
Supplementary Data from SGK2, 14-3-3, and HUWE1 Cooperate to Control the Localization, Stability, Function of Oncoprotein PTOV1
Supplementary Data from SGK2, 14-3-3, and HUWE1 Cooperate to Control the Localization, Stability, Function of Oncoprotein PTOV1
<div>Abstract<p>PTOV1 is an oncogenic protein, initially identified in prostate cancer, that promotes proliferation, cell motility, and invasiveness. However, the mechanisms regulate PTOV1 remain unclear. Here, we identify 14-3-3 as a interactor show high levels of expression, like PTOV1, correlate with cancer progression. We discover SGK2-mediated phosphorylation at S36, which required for binding. Disruption PTOV1–14–3-3 interaction results accumulation nucleus...
Abstract Cells must respond to changing environments by modulating signaling and gene expression patterns maintain homeostasis, health, viability. Inappropriate responses lead disease processes, such as cancer. Despite improvements in targeted treatment options, cancer remains the second leading cause of death United States, illustrating need develop new highly effective therapies. 14-3-3 interacts with a network proteins support pathways promoting oncogenesis, metastasis, growth, cellular...
Abstract PTOV1 is an oncogenic protein, initially identified in prostate cancer, that promotes proliferation, cell motility, and invasiveness. However, the mechanism of regulation poorly understood. To understand these mechanisms, we identify 14-3-3 as a interactor show high levels expression, like PTOV1, correlate with cancer progression. Further, found SGK2-mediated phosphorylation required for binding. This occurs cycle-dependent manner peaks G1 phase. Disruption PTOV1-14-3-3 interaction...
Abstract ACK1 is an oncogene in the ACK family of non-receptor tyrosine kinases (NRTK). In humans, located on chromosome 3q29, a region that frequently amplified variety cancers including prostate, lung and breast. The kinase has unique domain arrangement with, most notably, putative ubiquitin association (UBA) at their C-termini. present study, we focus understanding ubiquitin-binding nature UBA its role regulation. Structural modeling sequence analysis suggest diverges from many other UBAs...