Ahead, Marco Baptista, Ph D, Associate Director of Research Programs for the Michael J.
The techniques of immunocytochemistry and live cell imaging were used to visualize the effects of the inhibition of PDK1 on division in He La cells. The inhibited cells were unable to initiate anaphase cell-elongation ultimately leading to the flattening of spherical, metaphase cells.
Preliminary studies with imunocytochemistry and live cell imaging suggested that insulin treatment reversed PDK1 inhibition, but the results were not statistically significant.
Pathogenic fungi have diverse growth lifestyles that support fungal colonization on plants. doi: 10.1111/j.1365-2958.2006.05076.x Pub Med Abstract | Cross Ref Full Text | Google Scholar Gout, L., Kuhn, M.
Successful colonization and infection for all lifestyles depends upon the ability to modify living host plants to sequester the necessary nutrients required for growth and reproduction. L., Vincenot, L., Bernard-Samain, S., Cattolico, L., Barbetti, M., et al. Genome structure impacts molecular evolution at the Avr Lm1 avirulence locus of the plant pathogen Leptosphaeria maculans.
Fox Foundation for Parkinson’s Research, Glaxo Smith Kline, and Merck collaborated on the systematic testing that determined the LRRK2 kinase regulates cellular trafficking by deactivating certain Rab proteins (3, 8, 10 and 12). Fox Foundation, the newly discovered link between mutant LRRK2 and inappropriate deactivation of Rab function unlocks more than 20 years of accumulated knowledge of the roles of Rab proteins and may improve understanding of LRRK2 dysfunction in the Parkinson’s disease process.
The research group now is working to further characterize the Rab proteins modified by LRRK2 and to understand how an imbalance in cellular trafficking leads to the degeneration of neurons seen in Parkinson’s disease.
In recent years, leucine-rich repeat kinase 2 (LRRK2) mutations have been identified as having a central part in the development of Parkinson’s disease.
Efforts have since been underway to better understand LRRK2 and develop therapeutic interventions that inhibit LRRK2 kinase activity.
MEF2C is not degraded when co-expressed with MAML1 deletion constructs, MAML1 1-301 and MAML1 Δ75-300, suggesting the entire c-terminus is needed for degradation.