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- W2284529971 abstract "Germ line mutations in the human lkb1 gene are the main cause of the Peutz-Jeghers syndrome (Hemminki, 1999) and somatic lkb1 mutations are associated with mainly epithelial cancers (Sanchez-Cespedes, 2007). The serine/threonine kinase LKB1 (STK11) is involved in different cellular processes like cell proliferation, energy homeostasis and cell polarity (Martin-Belmonte and Perez-Moreno, 2012). Especially the observation that activation of mammalian LKB1 can polarize cells in absence of cell-cell contacts (Baas et al., 2004) has drawn attention to the role of LKB1 in cell polarity. Using Drosophila melanogaster and other model organisms various potential downstream targets have been identified, while little is known about its upstream regulation and the mechanisms by which LKB1 controls cell polarity. It has been suggested that LKB1 might be mostly constitutively active and that its involvement in specific responses depends on localization of it to specific subcellular compartments (Sebbagh et al., 2011). In order to study the role of LKB1 in cell polarity an antibody against LKB1 has been raised for this work that could detect LKB1 in different tissue of Drosophila. Remarkably, endogenous LKB1 localizes cortically in asymmetrically dividing embryonic neuroblasts but cytoplasmic in larval neuroblasts. LKB1 has been described to control asymmetric divisions in both of these cell types. How it can exert its functions with different localizations remains to be answered. Furthermore, endogenous LKB1 localizes to the basolateral cortex in embryonic epithelial cells. I observed that a farnesylation deficiency does not alter the localization of LKB1 remarkably in epithelial cells and did not affect its activity towards its downstream target AMPK (AMP-activated protein kinase). A polybasic motif was identified in this work, which interacts with phospholipids found in the plasma membrane and potentially with the newly identified interaction partners α-Spectrin and β-Spectrin. Furthermore, three nuclear localization signals (NLS) of Drosophila LKB1 were identified. A construct carrying mutations in all three NLS had a reduced ability to rescue an lkb1-KO mutant and revealed a lower basal activity towards its substrate AMPK in embryonic lysates. Moreover, the mutation of the three NLS decreased the phenotype of LKB1 overexpression in the negative regulation of organ size compared to its wild type counterpart." @default.
- W2284529971 created "2016-06-24" @default.
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- W2284529971 date "2016-01-08" @default.
- W2284529971 modified "2023-09-23" @default.
- W2284529971 title "Subcellular localization of LKB1 and characterization of its interactions with the membrane skeleton in Drosophila melanogaster" @default.
- W2284529971 hasPublicationYear "2016" @default.
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