The research projects within Ylva Ivarsson Group
The Ivarsson group has several on-going projects with focus on molecular interactions. We use proteomic peptide phage display to identify interactions of potential biological relevance, bioinformatics to filter for relevant binders and in vitro affinity measurements and cell-based assays for detailed analysis of key interactions. When appropriate, we also probe the interplay between peptide and phospholipid binding.
Interaction profiling through proteomic peptide phage display
A significant part of the human proteome is intrinsically disordered. These regions are enriched in short motifs serving as docking sites for peptide binding modules. Peptide-motifs interactions are crucial for the wiring of signaling pathways. These important but transient interactions are difficult to capture through most conventional high-throughput methods. We apply a novel approach for the large-scale profiling of domain-motifs interactions called Proteomic Peptide Phage Display (ProP-PD) (Ivarsson et al, 2014, Sundell & Ivarsson, 2014). The method allows the interrogation of domain-motifs interactions on a proteome-wide scale. ProP-PD can be used to search for protein-motif interactions of potential biological relevance on a proteome wide scale and it provides information that is complementary to other high-throughput methods.
Functional and structural analysis of syntenin interactions
We have a long-standing interest in the field of PDZ domains, ranging from folding to functional analysis (see list of publications). Currently, we are performing a detailed structure function analysis of the two closely linked PDZ domains of the adaptor protein syntenin. Syntenin is involved in processes regulating cell-cell adhesion, vesicular trafficking and synaptic transmission, and is upregulated in several cancers. Most syntenin ligands have been identified through yeast-two-hybrid experiments. We are currently expanding the syntenin network and perform detailed functional and structural analysis of key interactions.