Basement membranes are evolutionarily ancient extracellular matrices that play key roles in tissue morphogenesis and organogenesis. In C. elegans, late embryonic development involves elongation of the embryo from a comma shape to a worm shape. Many basement membrane components such as type IV collagen and Perlecan are required for embryonic elongation. We previously showed that Peroxidasin/PXN-2 and F-spondin/SPON-1 are essential for epidermal elongation (Gotenstein, et al. Development. 2010; Woo, et al Development. 2008). Peroxidasins are extracellular peroxidases thought to catalyze sulfilimine cross-linking of collagen IV in the basement membrane. Complete loss of function of PXN-2 causes nonconditional lethality and arrest in late embryogenesis. F-spondins are conserved ECM proteins whose mechanisms remain unclear. We report that such pxn-2 null mutant phenotypes can be suppressed to viability by gain of function mutations in a variety of extracellular matrix or cell-matrix receptor proteins. From large-scale screens for suppression of pxn-2 or spon-1 we identified over 30 suppressors, 12 of which result in missense alterations in the transmembrane protein myotactin/LET-805. The LET-805 extracellular domain contains at least 32 Fibronectin type III repeats (Hresko, et al. JCB. 1999); our suppressor mutations cluster in two pairs of repeats, suggesting these repeats may play a critical role in LET-805 function. let-805 null mutants are nonconditional embryonic lethal; whereas our suppressors are viable and display no obvious phenotypes other than suppression. We find that let-805 suppressor alleles partially suppress loss of function in other basement membrane components (type IV collagen) but not loss of function in intracellular epidermal cytoskeletal components (e.g. vab-19). Localization of a LET-805::GFP knockin is essentially normal in the suppressor alleles, suggesting they have a subtle effect on LET-805 expression. We will also present our analysis of additional suppressor loci from our screen. Our results reveal compensatory mechanisms in basement membrane receptor complexes that allow key structural or enzymatic components to be bypassed.