Thousand-and-one-amino-acid kinase 2 (TAOK2) is a member of the MAP kinase kinase kinase (MAP3K) family that plays critical roles in various physiological and pathophysiological cellular responses, such as regulation of microtubule dynamics and antiviral immunity. The literature links sensing of dsRNA and activation in innate immunity by TAOK2 to its interaction with the ubiquitin ligase protein TRIM4. However, the structural and mechanistic basis of these pleiotropic functions remains poorly understood, thereby presenting the field with a progress bottleneck. TAOK2 is the largest of three TAOK family members and features a conserved kinase domain (KD) coupled to a much larger segment predicted to adopt a coiled-coil (CC) region and an additional leucine-rich (Leu) region. These scaffolding parts of TAOK2 are thought to mediate interactions with TRIM4, dsRNA, and cellular membranes. At the same time, the most readily studied function of TAOK2 as a kinase via its conserved KD has not yet been linked to its much more substantial non-kinase segment. Here, we propose a doctoral research project at the forefront of molecular and structural biology to elucidate the structure-function landscape of TAOK2 and its complexes with TRIM4 and viral dsRNA. Such knowledge will provide insights into the modular function and mechanistic synergies comprised in the enigmatic structure of TAOK2, and will facilitate further interrogation of TAOK proteins in physiology and disease.