The conserved NDR-family kinase Sid2p localizes to the contractile ring during fission yeast cytokinesis to promote ring constriction, septation, and completion of cell division. Previous studies have found that the Type 2 interphase node proteins Blt1p and Gef2p contribute to localization of Sid2p and its regulatory protein Mob1p at the division site. However, their relative contributions and whether they operate in the same or parallel pathways has been unclear. In this study, we quantify the respective roles of Blt1p and Gef2p in Sid2p/Mob1p recruitment and characterize the effect of single and double deletion mutants on contractile ring dynamics and completion of cell division. Using quantitative confocal fluorescence microscopy, we measured Sid2p and Mob1p recruitment to the division site in blt1∆, gef2∆, and blt1∆/gef2∆ mutant cells. We observed an equivalent decrease in Sid2p/Mob1p localization for both single and double mutants. Though assembly of the contractile ring is normal in these mutants, the reduction in Sid2p/Mob1p at the division site delayed the onset of contractile ring constriction and completion of division. We quantified localization of Blt1p and Gef2p at the medial cortex throughout the cell cycle and found that Blt1p localization to interphase nodes and the contractile ring is independent of Gef2p. However, Gef2p localization to the contractile ring is decreased in blt1∆ mutants. Blt1p and Gef2p work in the same pathway, rather than in parallel, to localize the NDR-family kinase Sid2p and its regulatory partner Mob1p to the division site, thereby promoting timely completion of cell division. Future studies are necessary to understand how additional fission yeast cytokinesis proteins work with these Type 2 interphase node components to promote Sid2p/Mob1p recruitment.