Cryptococcus neoformans is a type of pathogenic fungi that can cause infections in people with weakened immune systems. This fungal pathogen can survive in the body by growing at the host's body temperature (37\'b0C), forming a carbohydrate capsule, and producing melanin. When Cryptococcus neoformans strains lack certain septin proteins, they cannot grow at 37\'b0C and are not able to cause infections in mice. However, it is not yet clear how septins help the yeast to grow at the host's body temperature. Septins are a group of proteins that are important for cell division and morphogenesis. In the model organism, Saccharomyces cerevisiae septins are essential. S. cerevisiae septins form a higher-order complex at the mother bud-neck to scaffold over 80 proteins, including those involved in cell wall organization, cell polarity, and cell cycle control. In C. neoformans, septins also form a complex at the mother bud neck but the septin interacting proteome in this species remains largely unknown. In this study, the entire septin complex in C. neoformans was uncovered as downregulated during the stationary growth phase and heat stress. In addition, we investigated the septin interactome in C. neoformans, shedding light on the proteins that interact with septins Cdc3 and Cdc10 under ambient temperature and heat stress, respectively. Our findings unveiled a diverse array of interacting proteins, including components of Golgi to plasma membrane transport, cell division, and single-stranded DNA binding. \'a0Overall, this study delineates septins in C. neoformans as part of the cytoskeleton and cytoskeleton-dependent cytokinesis and provides a landscape of septin interactors to investigate and further understand septin biology in fungal systems.