In JoVE (1)
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Articles by Yury Bodrov in JoVE
Comprehensive Characterization of Extended Defects in Semiconductor Materials by a Scanning Electron Microscope Ellen Hieckmann1, Markus Nacke1, Matthias Allardt1, Yury Bodrov1, Paul Chekhonin2, Werner Skrotzki2, Jörg Weber1 1Institute of Applied Physics, Semiconductor Physics, Technische Universität Dresden, 2Institut für Strukturphysik, Technische Universität Dresden The optical, electrical, and structural properties of dislocations and of grain boundaries in semiconductor materials can be determined by experiments performed in a scanning electron microscope. Electron microscopy has been used to investigate cathodoluminescence, electron beam induced current, and diffraction of backscattered electrons.
Other articles by Yury Bodrov on PubMed
Î²2-Syntrophin is a Cdk5 Substrate That Restrains the Motility of Insulin Secretory Granules PloS One. 2010 | Pubmed ID: 20886068 The molecular basis for the interaction of insulin granules with the cortical cytoskeleton of pancreatic Î²-cells remains unknown. We have proposed that binding of the granule protein ICA512 to the PDZ domain of Î²2-syntrophin anchors granules to actin filaments and that the phosphorylation/dephosphorylation of Î²2-syntrophin regulates this association. Here we tested this hypothesis by analyzing INS-1 cells expressing GFP-Î²2-syntrophin through the combined use of biochemical approaches, imaging studies by confocal and total internal reflection fluorescence microscopy as well as electron microscopy. Our results support the notion that Î²2-syntrophin restrains the mobility of cortical granules in insulinoma INS-1 cells, thereby reducing insulin secretion and increasing insulin stores in resting cells, while increasing insulin release upon stimulation. Using mass spectrometry, in vitro phosphorylation assays and Î²2-syntrophin phosphomutants we found that phosphorylation of Î²2-syntrophin on S75 near the PDZ domain decreases its binding to ICA512 and correlates with increased granule motility, while phosphorylation of S90 has opposite effects. We further show that Cdk5, which regulates insulin secretion, phosphorylates S75. These findings provide mechanistic insight into how stimulation displaces insulin granules from cortical actin, thus promoting their motility and exocytosis.