Microtubules are cytoskeletal components involved in many cell functions, including cell division, migration, and intracellular transport. In addition to their structural role, microtubules are dynamic. They can transition between phases of growth and shrinkage; this is the microtubule dynamic instability. In cells, this behavior is regulated by microtubule-associated proteins (MAPs). One of the main families of MAPs is the plus-end tracking proteins (+TIPs). +TIPs bind to a discrete region at the end of growing microtubules and are involved in the regulation of microtubule dynamics. The core members of this family are end-binding (EB) proteins; they can autonomously track growing microtubules and recruit other +TIPs to the microtubule plus end. For instance, they recruit cytoskeleton-associated protein-glycine-rich (CAP-Gly) domain proteins such as CLIP-170. CLIP-170 is the founder of this +TIP family, and it is a microtubule rescue factor. Apart from EB and CLIP, hundreds of +TIPs localize at the microtubule end. However, how they organize in a spatiotemporally regulated manner is still under investigation. Recently, phase separation (PS) has emerged as a mechanism for compartmentalization inside the cell. In opposition to membrane-bound organelles, phase-separated organelles assemble through a demixing process, forming two coexisting phases, a dilute phase and a dense phase. Nuclear speckles, stress granules, nucleoli, and Cajal bodies all form through PS; they are now widely called biomolecular condensates. Several MAPs undergo phase separation, promoting microtubule nucleation and protein organization on microtubules. In this thesis, we show that three canonical +TIPs, EB1, EB3, and CLIP-170, undergo phase separation in solution and on microtubules in vitro. This phase separation regulates microtubule dynamics, increasing growth speed and decreasing catastrophe frequency