Life Sciences & Biotechnology
Title : | Studies on protein complexes associated with RBR E3-Ubiquitin ligases |
Area of research : | Life Sciences & Biotechnology |
Focus area : | Proteomics |
Principal Investigator : | Dr. Maddika Subbareddy, Centre For DNA Fingerprinting And Diagnostics (CDFD), Hyderabad, Telangana |
Timeline Start Year : | 2023 |
Timeline End Year : | 2026 |
Contact info : | msreddy@cdfd.org.in |
Details
Executive Summary : | Ubiquitination is a reversible protein modification that plays a crucial role in cellular processes. Ubiquitin, a 76-aminoacid polypeptide, is attached covalently to substrates in an ATP-dependent manner through a sequential 3-step process mediated by three sets of enzymes: E1 activating enzyme, E2 conjugating enzyme, and E3 ligases. E3 ligases determine substrate specificity and diversity of ubiquitin chain linkages. They are classified into RING E3-ligases and HECT E3-ligases, and a third class, the RING-in between-RING (RBR) family, has been identified. The proposed work aims to understand the possible roles and regulation of RBR E3 ligases by dissecting protein complexes associated with different RBR E3-ligases. There are 14 RBR E3 ligases in humans, and using biochemical purification and proteomic approaches, the protein complexes associated with all RBR E3-ligases will be identified. The importance of these proteins will be characterized through biochemical and cellular assays. This proposal aims to uncover regulators and substrates linked with different RBR E3-ligases, potentially providing new possibilities for understanding ubiquitin-controlled cellular signaling. |
Total Budget (INR): | 66,89,347 |
Organizations involved