'Structural Investigation of the effect of Ser/Thr Phosphorylation of Sam68 on Splicing Activity'

Series Name Interdisciplinary Science Society
Speaker Jaelle Foot, Department of Biochemistry
Type Lectures & Talks
Starts at Mar 05, 2014 01:30 PM
Ends at Mar 05, 2014 02:30 PM
Venue F11, Physics and Astronomy building.
Open To University staff and students

The next academic seminar hosted by the Interdisciplinary Science Society is taking place on Wednesday the 5th of March. Jaelle Foot from the department of biochemistry will be giving a talk entitled 'Structural Investigation of the effect of Ser/Thr Phosphorylation of Sam68 on Splicing Activity', discussing how the many techniques found in a variety of disciplines are used and adapted to elucidate the molecular structure of large macromolecules. The seminar will be held at 1:30pm in f11 of the Physics and Astronomy building.

The aim of these seminars is to both increase the dialogue between undergraduates and PhD students, and to show students the many opportunities available in research that are not always obvious. All are welcome and refreshments will be available.

The STAR (Signal Transduction and Activation of RNA) family of proteins provide a clear link between alternative splicing and signal transduction. In particular, Sam68, the best-characterized member of this family, is subject to various post-translational modifications and affects a diverse range of cellular processes such as cell cycle regulation, apoptosis and differentiation, through its direct involvement in RNA export, signal transduction and alternative splicing. It has been shown that Sam68 has enhanced splicing activity following Serine/Threonine phosphorylation by kinases such as ERK, Cdc2 and Nek2. It is unclear, however, whether this affect is due to changes in RNA binding or in interactions with other members of the spliceosome.

We have shown by radioactive in vitro kinase assay that residues within the STAR (RNA binding) domain of Sam68 are phosphorylated by these kinases. Following assignment of a portion of the STAR domain, we are using NMR as a tool to determine specific sites of phosphorylation. In addition, we are investigating the mechanism of RNA binding to Sam68 using NMR, Xray crystallography and other techniques.

For any questions on any of the seminars hosted by the society, please contact David McDonagh at dm250@student.le.ac.uk.