Cytoplasmic dynein is a microtubule-based motor protein required for intracellular transport, cell polarization, directed cell movement, and mitosis. During mitosis dynein function is critical at the cell cortex, spindle poles, and kinetochores. Kinetochore dynein has been proposed to play a role in microtubule (MT) attachment, chromosome congression, anaphase chromosome movement, and regulation of the spindle assembly checkpoint (SAC). Several proteins have been implicated in targeting or retaining dynein at kintechores during these activities; however, mechanisms which coordinate kinetochore dynein targeting and function remain unclear. Previous work identified a novel mitotic-specific phosphorylation site in the dynein intermediate chains (ICs) at threonine 89 (T89). Immunofluorescence microscopy (IFM) studies utilizing an antibody against phosphorylated dynein intermediate chain (PT89) has revealed dynein localizes to kinetochores at pro- metaphase and is progressively dephosphorylated in response to MT attachment, tension, and the kinetochore phosphatase PP1ÌÄå_Ìâå_. In contrast to existing models, initial dynein loading onto kinetochores does not require dynactin but rather a novel phosphorylation-specific interaction with zw10. Dephosphorylation switches binding to dynactin which is coupled to transport. This is consistent with dynein's proposed role in stripping checkpoint proteins from metaphase kinetochores. In addition to identifying PP1ÌÄå_Ìâå_ as the dynein phosphatase, Aurora B and Plk1 have emerged as candidate dynein kinases. Inhibitor studies revealed a requirement for both Aurora B and Plk1 in dynein kinetochore recruitment. Furthermore, in vitro kinase (IVK) assays suggest a role for Plk1 and not Aurora B in generation of the PT89 epitope. Spindly is a novel component of the dynein pathway during mitosis and is implicated in linking dynein to kinetochores. However, the specific contributions of Spindly to dynein function are not understood. shRNA-based depletion of Spindly revealed a novel role in anchoring dynactin and the dynactin-dependent population of dynein at kinetochores. In summary, dynein is initially recruited to unattached kinetochores as a phosphoprotein but undergoes dephosphorylation in response to chromosome alignment and this transition induces dynein's poleward motility which functions to silence the SAC. Overall, these findings provide a better understanding of how kinetochore dynein targeting and function is regulated by phosphorylation.