Publications by authors named "Shauna C Otto"
Article Synopsis
- Ligands like insulin and growth factors activate receptor tyrosine kinases (RTKs) at the cell membrane, which are key for converting external signals into internal responses.
- * RTKs interact with multiple signaling pathways (e.g., MAP/ERK, PLCγ, PI3K), making it difficult to study their individual effects.
- * The study employed optogenetics and click chemistry to selectively activate PI3K, revealing that its activation alone can successfully promote the movement of TRPV1 ion channels and insulin receptors to the plasma membrane.
With the great progress on determining protein structures over the last decade comes a renewed appreciation that structures must be combined with dynamics and energetics to understand function. Fluorescence spectroscopy, specifically Förster resonance energy transfer (FRET), provides a great window into dynamics and energetics due to its application at physiological temperatures and ability to measure dynamics on the ångström scale. We have recently advanced transition metal FRET (tmFRET) to study allosteric regulation of maltose binding protein and have reported measurements of maltose-dependent distance changes with an accuracy of ∼1.
View Article and Find Full Text PDFWith the great progress on determining protein structures over the last decade comes a renewed appreciation that structures must be combined with dynamics and energetics to understand function. Fluorescence spectroscopy, specifically Förster resonance energy transfer (FRET), provides a great window into dynamics and energetics due to its application at physiological temperatures and ability to measure dynamics on the ångström scale. We have recently advanced transition metal FRET (tmFRET) to study allosteric regulation of maltose binding protein and have reported measurements of maltose-dependent distance changes with an accuracy of ~1.
View Article and Find Full Text PDFArticle Synopsis
- Ligands like insulin and nerve growth factor bind to receptor tyrosine kinases (RTKs) at the cell membrane, initiating important cellular signals.
- RTKs, along with G-protein coupled receptors, are key players in converting external signals into internal responses, but studying their signaling has been complicated by their multiple downstream pathways.
- The research employed optogenetic techniques to specifically activate the PI3K pathway, showing that this activation alone can effectively transport TRPV1 ion channels and insulin receptors to the cell membrane without triggering other signaling pathways.
Dysferlin is a large membrane protein found most prominently in striated muscle. Loss of dysferlin activity is associated with reduced exocytosis, abnormal intracellular Ca2+ and the muscle diseases limb-girdle muscular dystrophy and Miyoshi myopathy. The cytosolic region of dysferlin consists of seven C2 domains with mutations in the C2A domain at the N-terminus resulting in pathology.
View Article and Find Full Text PDFMechanical stress on sarcolemma can create small tears in the muscle cell membrane. Within the sarcolemma resides the multidomain dysferlin protein. Mutations in this protein render it unable to repair the sarcolemma and have been linked to muscular dystrophy.
View Article and Find Full Text PDFIodinated pharmaceuticals, thyroxine (a thyroid hormone) and diatrizoate (an iodinated X-ray contrast medium), are among the most prescribed active pharmaceutical ingredients. Both of them have been reported to potentially disrupt thyroid homeostasis even at very low concentrations. In this study, UV-254 nm-based photolysis and photochemical processes, i.
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