5AAQ
TBK1 recruitment to cytosol-invading Salmonella induces anti- bacterial autophagy
Summary for 5AAQ
| Entry DOI | 10.2210/pdb5aaq/pdb |
| Related | 5AAS 5AAY 5AAZ |
| NMR Information | BMRB: 25734 |
| Descriptor | CALCIUM-BINDING AND COILED-COIL DOMAIN-CONTAINING PROTEIN 2, ZINC ION (2 entities in total) |
| Functional Keywords | calcium-binding protein, tbk1, ndp52, zinc-finger |
| Biological source | HOMO SAPIENS (HUMAN) |
| Total number of polymer chains | 1 |
| Total formula weight | 6866.30 |
| Authors | Thurston, T.L.,Allen, M.D.,Ravenhill, B.,Karpiyevitch, M.,Bloor, S.,Kaul, A.,Matthews, S.,Komander, D.,Holden, D.,Bycroft, M.,Randow, F. (deposition date: 2015-07-28, release date: 2016-07-13, Last modification date: 2024-05-15) |
| Primary citation | Thurston, T.L.,Boyle, K.B.,Allen, M.,Ravenhill, B.J.,Karpiyevich, M.,Bloor, S.,Kaul, A.,Noad, J.,Foeglein, A.,Matthews, S.A.,Komander, D.,Bycroft, M.,Randow, F. Recruitment of Tbk1 to Cytosol-Invading Salmonella Induces Wipi2-Dependent Antibacterial Autophagy. Embo J., 35:1779-, 2016 Cited by PubMed Abstract: Mammalian cells deploy autophagy to defend their cytosol against bacterial invaders. Anti-bacterial autophagy relies on the core autophagy machinery, cargo receptors, and "eat-me" signals such as galectin-8 and ubiquitin that label bacteria as autophagy cargo. Anti-bacterial autophagy also requires the kinase TBK1, whose role in autophagy has remained enigmatic. Here we show that recruitment of WIPI2, itself essential for anti-bacterial autophagy, is dependent on the localization of catalytically active TBK1 to the vicinity of cytosolic bacteria. Experimental manipulation of TBK1 recruitment revealed that engagement of TBK1 with any of a variety of Salmonella-associated "eat-me" signals, including host-derived glycans and K48- and K63-linked ubiquitin chains, suffices to restrict bacterial proliferation. Promiscuity in recruiting TBK1 via independent signals may buffer TBK1 functionality from potential bacterial antagonism and thus be of evolutionary advantage to the host. PubMed: 27370208DOI: 10.15252/EMBJ.201694491 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
Download full validation report
