Doublecortin-like kinase 1 (DCLK1), a bi-functional protein classified as a Microtubule-Associated Protein (MAP) and as a serine/threonine kinase, plays a critical role in regulating microtubule (MT) assembly. The DCX domains (DCX1 and DCX2) of DCLK1 are highly conserved with Doublecortin, a neuronal MT-stabilising protein. DCLK1 was first identified as a brain-specific protein playing a critical role in neurogenesis. However, over the past decade, overexpression of DCLK1 and DCLK1 mutations have been associated with various human cancers. Our present understanding of how DCLK1 dysfunction leads to tumourigenesis is limited and hampered by a lack of structural and functional information. We hypothesize that the conformational states of DCLK1, dictated by its kinase activity, represent a critical regulatory process that determine its MT binding function and signal output. Cryo-electron microscopy studies at 8Å resolution of Doublecortin bound to MTs have shown how the two DCX domains bind specifically to 13-pf MTs, and “staple” protofilaments [1], however whether DCX1 or DCX2 domain directly engage with MTs is still under debate. Additionally, DCLK1 and Doublecortin have a 50 amino acid N-linker preceding the DCX domains and a C-terminal PEST linker comprising phosphorylation sites whose function is currently unknown. We hypothesise that the presence of the kinase domain of DCLK1 will aid in stabilisation of DCX-tubulin interaction and provide a mean to elucidate the molecular basis for MT assembly by DCLK1 and more broadly the DCX containing proteins. We have begun to biochemically characterise DCLK1 and solved the first crystal structure of DCLK1 kinase domain. Additionally, we have shown how kinase activity negatively regulates tubulin polymerisation [2]. Here we summarise the current structural understanding of DCX binding to MTs and present our data on MT polymerisation in the presence of DCLK1.