Cells have an intrinsic ability to rapidly respond to changes in environment to affect cell cycle progression, membrane organisation and thereby regulate cell growth and division. The actin cytoskeleton is a highly dynamic complex of proteins which can rapidly reorganise to change the growth pattern of a cell. Class I myosins are monomeric actin associated motor proteins that play key roles in diverse cellular functions including tension sensing, membrane reorganisation, and promote actin polymer nucleation at sites of cell growth. We have undertaken a microscopy-based localisation and functional study of both C. elegans class 1 myosins, Hum-1 (Myo1eHum-1) and Hum-5 (Myo1dHum-5). Both motors are non-essential, and while Myo1eHum-1 is expressed and localises in diverse cells and tissues, Myo1dHum-5 localises exclusively to a subset of cells in the nervous system. While deleting the HUM-5 gene had no discernible effect upon the health or lifecycle of the worm, animals lacking Myo1eHum-1 displayed a reduced maximal brood size and a delay in embryo release. Using both fission yeast and nematode model systems we explored whether phosphorylation of a conserved serine residue within the Myo1e TH1 domain had an impact upon the localisation and function of the motor protein across eukaryotes. Using both nematode worm and fission yeast model systems we will share data that illustrates phosphorylation of this conserved residue modulates the ability of Myo1e to interact with phospholipids at cellular membranes, and thereby function, in. And thus, we conclude that TH1 domain phosphorylation is likely to play a key role in regulating the cellular distribution and function of Myo1e motors across all eukaryotes.