Articles by Kanwardeep S. Kaleka in JoVE
Pull-down of Calmodulin-binding Proteins Kanwardeep S. Kaleka1, Amber N. Petersen1, Matthew A. Florence1, Nashaat Z. Gerges1 1Department of Cell Biology, Neurobiology and Anatomy, Medical College of Wisconsin Calmodulin (CaM) pull-down assay is an effective way to investigate the interaction of CaM with various proteins. This method uses CaM-sepharose beads for efficient and specific analysis of CaM-binding proteins. This provides an important tool to explore CaM signaling in cellular function.
Other articles by Kanwardeep S. Kaleka on PubMed
Neurogranin Phosphorylation Fine-tunes Long-term Potentiation The European Journal of Neuroscience. Jan, 2011 | Pubmed ID: 21198977 Learning-related potentiation of synaptic strength at Cornu ammonis subfield 1 (CA1) hippocampal excitatory synapses is dependent on neuronal activity and the activation of glutamate receptors. However, molecular mechanisms that regulate and fine-tune the expression of long-term potentiation (LTP) are not well understood. Recently it has been indicated that neurogranin (Ng), a neuron-specific, postsynaptic protein that is phosphorylated by protein kinase C, potentiates synaptic transmission in an LTP-like manner. Here, we report that a Ng mutant that is unable to be phosphorylated cannot potentiate synaptic transmission in rat CA1 hippocampal neurons and results in a submaximal expression of LTP. Our results provide the first evidence that the phosphorylation of Ng can regulate LTP expression.