Projects per year
Abstract / Description of output
demonstrated that endogenous AGR2 and EpCAM protein associate in cells. Introducing a single alanine mutation in EpCAM at Tyr251 attenuated its binding to AGR2 in vitro and in cells. Hydrogen-deuterium exchange mass spectrometry was used to identify a stable binding site for AGR2 on EpCAM, adjacent to the TLIYY motif and surrounding EpCAM’s detergent binding site. These data define a dominant site on AGR2 that mediates its specific peptidebinding function. EpCAM forms a model client protein for AGR2 to study how an ER-resident
chaperone can dock specifically to a peptide motif and regulate the trafficking a protein destined for the secretory pathway.
FingerprintDive into the research topics of 'The sequence-specific peptide-binding activity of the protein sulfide isomerase AGR2 directs its stable binding to the oncogenic receptor EpCAM'. Together they form a unique fingerprint.
- 2 Finished
1/08/10 → 31/07/13
RASOR-Radical Solutions for Researching the Proteome: Interdisciplinary Research Collaboration in proteomic technologies
1/08/05 → 31/10/11
- Deanery of Molecular, Genetic and Population Health Sciences - Chair of Cancer Research
- Edinburgh Cancer Research Centre
Person: Academic: Research Active