Although mTOR is a known regulator of the cell size and Lkb1 can suppress mTOR via AMPK phosphorylation we did not find evidence of mTOR machinery misregulation in our model suggesting relatively intact energy sensing mechanisms. Remarkably, given that Lkb1 has been implicated in maintenance of polarity, we did not observe any obvious Rebaudioside-C perturbations in polarity in the intestinal epithelium. It remains possible that subtle changes are occurring in the absence of Lkb1, but that these do not result in obvious changes to brush border structure and nuclear localization. In summary, we show a complex sequence of events immediately following loss of function of Lkb1 leading to the inappropriate differentiation of secretory cells associated with abnormal expression of Notch pathway elements and consistent with many features of Notch pathway improper regulation. Our studies therefore reveal a critical role for Lkb1 in maintaining normal gut homeostasis.The two ALAS isoenzymes are translated as precursor proteins with N-terminal mitochondrial matrix import signal sequences that are proteolytically cleaved following importation to yield the mature enzymes. The activity of the enzyme is only manifested upon localization to the mitochondrial matrix, as this is where the substrate succinyl-CoA is produced. The internal cavities of organ systems are similarly lined and compartmentalized into functionally distinct partitions through the selective regulation of ionic and molecular exchange between luminal and interstitial compartments,Rebaudioside-A thus creating separated tissue microenvironments. Central to this permeability barrier function is the organization of individual epithelial cells into an epithelial sheet by cell-cell junctions that regulate paracellular movement and the coordinated apico-basal polarization of this sheet into functionally discrete subcellular regions, which facilitate vectorial transcellular transport.