The spindle assembly checkpoint (SAC) is a fundamental mitotic regulator that maintains genome stability by ensuring the fidelity of chromosome segregation. Defects in SAC surveillance can lead to aneuploidy, while several major chemotherapeutics (e.g. Taxol) rely on SAC-mediated mitotic arrest. The strength of the SAC varies between cell types and organisms, yet the reason for these differences is poorly understood. We have recently characterized SAC activity in C. elegans germline stem and progenitor cells (GSPCs) using in situ live-imaging of GSPC mitosis in whole-mount animals. Our work indicates that the SAC is stronger in GSPCs than in early embryonic blastomeres, providing a platform to dissect how SAC activity can vary between cell types and to uncover stem cell-specific adaptations. GSPCs are derived from an embryonic germline founder cell that is specified by a series of asymmetric cell divisions that are regulated by the highly conserved PAR polarity proteins. We used a fast-acting temperature-sensitive mutation that triggers a SAC response by inducing monopolar spindles, combined with live imaging, to determine whether the strength of the SAC varies between different cell lineages during embryogenesis. In agreement with a recent report, we found that the strength of the SAC scales with cell size, with smaller cells showing a stronger SAC response. Interestingly, however, cells in the germline lineage have a stronger SAC than would be predicted based solely on cell size. We found that enhanced checkpoint activity at the two-cell stage, in the smaller germline P1 blastomere, relative to its larger somatic sibling (AB), is only partially dependent on cell size, indicating that increased SAC activity in P1 depends on the asymmetric partitioning or control of checkpoint regulators. Indeed, in the absence of PAR proteins, when differences in both cell size and asymmetric segregation of cell fate determinants are disrupted, the SAC response in P1 and AB is identical. Neither MDF-1 nor BUB-3, two core SAC proteins, are enriched in P1 relative to AB, suggesting that enhanced SAC activity in P1 may be achieved via means other than simply increasing the concentration of SAC proteins. We are currently investigating whether recruitment of SAC proteins to unattached or improperly attached chromosomes differs between AB and P1. Altogether, our results suggest that enhanced SAC regulation may be a feature of germline cells throughout development and point to a novel interaction between PAR polarity regulators and the SAC.