Surprisingly, removal of in tissue with increased aPKC activity results in mild tissue overgrowth, indicating that in this context acts as a tumor suppressor. the SARAH domain name. In doing so, dRASSF inactivates the Hpo kinase cascade, thereby increasing Yki activity and promoting tissue growth . Recent studies in have identified a phosphatase complex, dSTRIPAK (Striatin-interacting phophatase and kinase) that directly binds dRASSF, dephosphorylates Hpo and restricts the activity of the pathway to promote tissue growth . Thus, Hpo activity is usually regulated by a variety of inputs from the cell membrane, and more directly via association with dRASSF and the dSTRIPAK complex. It has long been acknowledged that loss-of-function mutations in the apico-basal cell polarity gene result in tissue overgrowth and neoplastic tumors . We have shown in the developing vision that loss of and the concomitant increase in aPKC activity results in ectopic cell proliferation and suppression of developmental cell death (apoptosis) via impairment of the Hpo pathway, as assessed by decreased phospho-Yki and increased expression Topotecan of target genes (and tissue ectopic expression of Hpo pathway targets were normalized and overgrowth was decreased, showing that Yki activation was rate-limiting for the tissue overgrowth phenotype conferred by Lgl depletion . We also observed that Lgl/aPKC activity regulates the localization of Hpo/dRASSF . Here we further dissect the relationship between Topotecan Lgl/aPKC and Hpo pathway regulation. We show that Lgl/aPKC regulate the Hpo pathway independently of upstream components Excess fat and Kibra/Ex/Mer, the dSTRIPAK complex and dRASSF. Furthermore, Topotecan in the context of increased aPKC activity appears to have a tumor suppressor function. 2. Experimental 2.1. Travel Culture, Overexpression, and Clonal Analysis Mitotic vision clones and mosaic analysis with a repressible marker (MARCM) clones were generated as previously described . Clonal and MARCM crosses were raised at 25 C. Overexpression crosses with were undertaken at 18 C. 2.2. Travel Stocks (Kieran Harvey, Peter MacCallum Cancer Centre, Melbourne, Australia); (Bloomington Stock Centre, Bloomington, IN, USA); (Sonsoles Campuzano, Centro de Biologa Molecular Severo Ochoa, Madrid, Spain); (Nicholas Tapon, Cancer Research, London, UK); (Hugo Stocker, Institute of Molecular Systems Biology, Zurich, Switzerland); (Kenneth Irvine, The State University of New Jersey, New Brusnwick NJ, USA); (Duojia Pan, Johns Hopkins University School of Medicine, Baltimore, MD, USA); (Bruce Hay, California Institute of Technology, Pasadena, CA, USA); (Bruce Edgar, Fred Hutchinson Cancer Research Center, SPTAN1 Seattle, WA, USA); (Virender Sahota, Peter MacCallum Cancer Centre, Melbourne, Australia) this study; (National Institute of Genetics (NIG), Shizuoka , Japan); (Vienna RNAi Centre (VDRC), Vienna, Austria). 2.3. Immunohistochemistry, Imaging and Antibodies Larval and pupal discs were dissected and fixed as previously described . For Hpo, dRASSF, Cka and Mob4 staining, tissues were fixed in paraformaldehyde lysine periodate (PLP). Labeled samples were cleared through 80% glycerol and mounted. For Physique 1, Physique 2E, Physique 3A,C, Appendix Physique A1B,C, and Physique 4A,B images were collected on Biorad MRC1000 (Bio-Rad Laboratories, Hercules, CA, USA). Physique 2B, Physique 3B and Appendix Physique A1A were collected on an Olympus FV1000 (Olympus, Center Valley, PA, USA). Images in Physique 2C,D and Physique 4GCI were taken on a Nikon Eclipse 90i (Nikon, New York, NY, USA). Images were processed using Fiji, and assembled with Adobe Photoshop CS6 and Adobe Illustrator CS6. Adult eyes were imaged with a Scitec Infinity1 camera (Lumenera, Ottawa, Canada). Open in a separate window Physique 1 regulates the Hippo (Hpo) pathway in parallel with and E-cadherin (DE-Cad) antibodies that localize to the adherens junction and mark cell outlines. (ACE) mutant tissue lacks the expression of green fluorescent protein (GFP) and is.
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- Abbreviations: CON, control; CANA, canagliflozin; AMPK, AMP-activated proteins kinase; ACC, acetyl-CoA carboxylase
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