Scheid Signalling Lab @ York University

Our lab is focused on understanding cell signalling that controls cell division and apoptosis. We use primarily biochemistry and molecular biology to piece together receptor-to-gene expression pathways. Some of the projects in our lab include:

PDK1 – The 3-phosphoinositide dependent kinase-1 is an important activator of serine/threonine kinases of the AGC kinase family and in particular PKB/Akt. Our work with PDK1 has sought to understand its localization in the cell, post-translational events that change its activity, and new substrates that it might phosphorylate. See Moon et al., and Scheid et al. and Sephton et al. for our publications on PDK1.

MEKK2/3 – The stress-activated kinases MEKK2 and MEKK3 act downstream of a host of cellular receptors and inputs, leading to a wide array of gene expression. Our work has focused on understanding the biochemistry of MEKK2 and MEKK3 interaction with 14-3-3 proteins. See Matitau and Scheid.

ROCK – The Rho-associated coil-coiled kinase is an important downstream target of the small G-   protein Rho. It functions to alter the cytoskeleton by phosphorylating components that alter actin and myosin polymerization. We showed that the hydrophobic motif of ROCK in the kinase domain interacts with an N-terminal extension, and this is required for activity. Small molecule inhibitors of this interaction could help in the control of metastasis during cancer. See Couzens et al.

CDCA7 – Cell division control associated protein-7 is a new transcription factor that interacts with the potent oncogene Myc. We have discovered that CDCA7 is phosphorylated and this controls its interaction with Myc and its localization within the nucleus. Current efforts in the lab are aimed at understanding the mechanism by which phosphorylation alters Myc-CDCA7 binding and localization.

For a complete list of our labs publications, see here.