The double lipid bilayer of the nuclear membrane serves as a physical barrier to restrict access of macromolecules to genetic material inside the nucleoplasm in all eukaryotes. Compartmentalization is at the heart of transcriptional and translational control. However, the nuclear envelope (NE) represents an obstacle to cells during mitosis since the cytoplasmic cytoskeleton must interact with nuclear DNA to ensure accurate chromosome segregation. In most higher eukaryotes, the spindle forms after NE fragmentation in early mitosis, but, in fungi the NE remains intact throughout cell division and yeast microtubule organizing centers, known as spindle pole bodies (SPBs), gain access to chromosomes via insertion into the NE. Membrane insertion of SPBs is thought to be mechanistically similar to that of de novo nuclear pore complex (NPC) assembly, yet how both complexes interact with the NE to promote cell cycle specific changes in its structure is poorly understood. Central to addressing this question is the ability to 1) visualize assembly intermediates and 2) detect proteins that localize permanently or transiently to these structures. Because Saccharomyces cerevisiae and Schizosaccharomyces pombe SPBs are roughly ten times larger than the NPC, they were ideal to investigate how complexes are assembled into the NE. Using biochemical and genetic approaches combined with super-resolution microscopy, we have identified factors that localize transiently or permanently to SPBs as they are inserted into the NE. These proteins are leading candidates to convert the planar NE into a highly curved pore membrane. Using epistasis and co-localization studies, we have put factors into an assembly pathway and have used mutant alleles to provide evidence that some lead to localized changes in NE structure. Determining how SPBs interact with the NE will provide insight into the ways that their metazoan counterparts (centrosomes) regulate their numbers and control events such as NE breakdown.