we analyzed the kinase activity in lesioned wild type NgR EH co cultures

recent reports have called into question whether Akt is truly a essential effector of PI3K process driven oncogenesis. More over, emerging data suggest that c-Met Inhibitors Akt inhibitors could be of limited clinical utility in cancers driven by mutations in PTEN. Hence, the degree to which Akt is really a expected effector of PTEN tumefaction suppression is not clear at the moment. How may abrogation of cell size check-point control really push neoplasia We hypothesize that the explanation may be associated with the eukaryotic cell gate that stops cell division in the level of the cell cycle until cells reach adequate size to split up their biomass into two daughter cells. Although in normal-sized cells, this checkpoint is vigilant in avoiding proliferation and cell division, in large PTENdeficient cells, cells may be permitted by this checkpoint to enter the cell cycle, causing increased proliferation and neoplasia. This theory, but, remains experimentally untested. In addition to showing that Akt is dispensable Organism for cell size checkpoint control, we discovered actin remodeling as a vital PTEN controlled process that is associated with regulating cell size control. These results are in keeping with early work of Goberdhan et al., who demonstrated that in D. melanogaster, PTEN affects cytoskeletal organization in multiple cell types. Here we have discovered an actual interaction between PTEN and an actin remodeling complex which includes actin, actin, and many actin remodeling proteins, including EPLIN and gelsolin. This finding raises still another unresolved question: which of those proteins interacts directly with PTEN We suppose that Ibrutinib PTEN interacts specifically with actin and ultimately with the meats, since actin appears to be the most abundant protein in PTEN immunoprecipitates. Furthermore, PTEN includes a domain with homology to tensin, a known actin interacting protein. A definitive response to this problem will require the capacity to recapitulate the interactions with purified components, and these efforts are ongoing in our laboratory. This recently identified conversation between PTEN and the actin remodeling complex is reminiscent of the current work of van Diepen et al., who demonstrated that PTEN interacts with myosin V in neurons. These researchers further showed this interaction is critical for the ability of PTEN to manage how big is these neurons. While we did not particularly identify myosin V like a PTEN interacting protein in our study, we speculate that this omission is due to cell-type specific differences in the expression pattern of the myosin V gene. Determination of whether myosin V is part of a larger actin containing complex within the nerves used in this study is going to be interesting.