ILSC Monthly Seminar: March 2011Combining Bioinformatics and Proteomics to Identify Potential Biological Substrates for a Family of Membrane-bound Aspartyl Proteases
Time/Place: Thursday, March 31st at 3:00 pm, 130 SMed Abstract: The deposition of the short peptide beta amyloid (Aβ) in the brain leads to the development of Alzheimer's disease (AD). Aβ is a product of a sequential cleavage of the amyloid precursor protein (APP) by the proteases β-secretase and γ-secretase. BACE1, a type I transmembrane aspartyl protease, has been characterized as the β-secretase and, as such, is a promising therapeutic target for the chronic treatment of AD. However, few substrates have been identified and the physiological function of BACE1 remains elusive. BACE2 is a close homolog of BACE1 with 50% sequence identity and a very similar 3D structure. BACE2 also shows some modest β-secretase activity but no native substrates have been identified other than APP. We hypothesize that BACE1 and BACE2 have similar but distinct functions in biological systems, and that identification of potential substrates for this family of aspartyl proteases will provide valuable insights into their biological functions. This study focuses on identifying putative in vivo protease substrates by combining bioinformatics and proteomics data. |
2013January: Michael TaylorFebruary: Marna Yandeau-Nelson March: Paul Lockman April: Martin Gruebele 2012January: David D. Thomas 2011January: Clay CarterFebruary (a): Anne Kenworthy February (b): Jennifer Liang March: Joe Johnson April: Marco Ciufolini May: Gary Pielak October: Matthew Andrews December: Andrew Skildum 2010November: Rui WangOctober: Marshall Hampton |