Christian Randal Marks, BA
Graduate Student, Colbran laboratory, Molecular Physiology & Biophysics
- : christian.r.marks@Vanderbilt.Edu
- :
724 Robinson Research Building
Calcium/calmodulin-dependent kinase II (CaMKII) is a highly abundant serine/threonine kinase in the brain. Direct interactions between activated CaMKII and its substrates play a number of important roles within the cell such as feedback regulation of channels/receptors, and normal synaptic plasticity. Relatively few CaMKII-associated proteins are known to preferentially interact with inactive CaMKII, and their functional roles are poorly understood. Moreover, molecular mechanisms underlying the coupling of CaMKII to the G-protein coupled receptors (GPCRs) that stimulate the release of intracellular calcium are poorly characterized. An interaction between inactive CaMKII and the metabotropic glutamate receptor 5 (a Gq-coupled GPCR) was recently reported. I am currently investigating how CaMKII interactions with mGlu5 can change mGlu5 signaling. Understanding the physiological importance of this interaction may lead to novel treatments of neurological disorders linked to dysfunction of mGlu5 such as Parkinson’s Disease, addiction, schizophrenia, and autism spectrum disorder.