Short report by Henrike Indrischek: Binding Capability of Visual Arrestins to the Coated Pit Machinery at Vanderbilt University (May 05 – July 28)
by Henrike Indrischek (phd student at Leipzig University): During my research stay at Vanderbilt university this summer, I worked on the biochemical characterization of the interaction of clathrin and visual arrestin in the laboratory of Seva Gurevich and the modeling of this interaction with computational methods in the laboratory of Jens Meiler.
The cytosolic arrestin proteins mediate desensitization of activated G protein-coupled receptors (GPCRs) via competitive binding to the active phosphorylated receptor. As different arrestin conformations can result in specific signaling outcomes, this protein family is an attractive target in drug therapeutics. Non-visual arrestins mediate uptake of the receptors into the cell by also binding clathrin, a component of the endocytosis machinery. Conservation of the low affinity clathrin binding site of one of the visual arrestins suggested a possible role in clathrin-mediated endocytosis. I wanted to use the reasearch stay at Vanderbilt to follow up on this hypothesis with biochemical and computational methods from structural biology.
I especially enjoyed spending time in an experimental laboratory working ‘hands-on’ again after a long time of computational work. The people in the Gurevich lab did an excellent job in welcoming me in the group and in explaining me methods and techniques, that I had not used in a long time, e.g. Western Blot. Apart from the scientific experience, I spent a really good time with amazing people, both from the Meiler and Gurevich lab! This included typical American activities like watching a baseball game, eating out at Southern style restaurants, having a BBQ, going out on Nashville’s famous broadway. Everybody has been very friendly (definitely exceeding Southern style-small talk friendliness) so that leaving Nashville also ment leaving new and old friends. – Thank you, Sandra, Sergey and Alyssa!!!