We hypothesized that remodeling could alleviate SPB damage in these strains either by growth, which could add new Spc110, or by exchange, which could replace damaged Spc110 with functional Spc110. Secondary screens identified four genes required for SPB remodeling. UBC4 is required to maintain SPB size during the cell cycle, and NCS2, POM152, and NUP60 are required for SPB growth during a mitotic cell cycle arrest. SPB remodeling has been shown to occur at discrete times during the cell cycle. However, very little is known about the process of remodeling and the proteins involved in regulating and facilitating SPB growth and component exchange. In this study, we have identified several candidates for involvement in the SPB remodeling process. Proteins identified include microtubule motors, protein modification enzymes, and nuclear pore proteins. Many of the yeast microtubule motors were identified and had a synthetic growth defect with Spc110 cleavage. This information, coupled with previous studies on motors in other organisms, suggests that motors play a role in assembly of the spindle and specific SPB components. Dynein and Ncd have previously been shown to move microtubule bundles to the centrosome in Drosophila, and dynein has also been shown to transport pericentrin and c-tubulin to the centrosome in mammalian cells. While deletion of the motors identified in our study did not lead to a defect in SPB growth during metaphase arrest, further characterization of these proteins and their roleinSPB remodeling could shed light on the process of spindle assembly. Our secondary screens identified four proteins that regulate SPB size: Ncs2, Nup60, Pom152, and Ubc4. Loss of Ncs2, Nup60, or Pom152 led to an impaired ability to increase SPB size during metaphase arrest, implicating these proteins in SPB component assembly. Ncs2 is involved in the ubiquitin-related modifier Urm1 pathway and is necessary for thiolation of Lys and Glu tRNAs. Ncs2 has no known association with SPB proteins. However, our results suggest involvement of the urmylation pathway in regulation of SPB size. Components of the urmylation pathway have been previously shown to have genetic interactions with nuclear pore component NUP133: deletion of URM1 or UBA4 leads to a synthetic growth defect when combined with NUP133 deletion. Furthermore, deletion of NUP133 is synthetic lethal with deletion of another nuclear pore component gene, NUP60. We have shown that Nup60 and Pom152 are necessary for surviving Spc110 cleavage and for SPB growth during metaphase arrest. The only protein previously described as having a role in assembly of SPB components is nuclear pore protein Mlp2. We found that mlp2D does not have a synthetic growth defect when combined with Spc110 cleavage and U0126 therefore was not found in our SGA screen. However, attachment of Mlp2 to the nuclear pore is mediated by Nup60. Pom152 has previously been shown to form a complex with Ncd1 and Pom34, which assembles to form a ring around the nuclear membrane structure of the pore.