Date of Award


Degree Type


Degree Name

Master of Science




Dr. Susan Meakin

Second Advisor

Dr. Eric Ball

Third Advisor

Dr. Shawn Li


We believe that ShcC contributes to dephosphorylation of NMD A receptors. ShcC7' mice have increased levels of neuronal NR2B tyrosine phosphorylation and increased hippocampal long term potentiation. Our data demonstrates this increased phosphorylation is of tyrosine 1472 of NR2B indicating prolonged activity of the NMDA receptor. The data presented indicates that the ShcC SH2 domain does have the ability to interact with at least four tyrosine phosphorylated proteins and I have also identified at least three novel binding partners of ShcC: NKAIN2, Ubiquitin thiolesterase, and a protein similar to Glycoside hydrolase family 2 TIM barrel. Finally, it has been conclusively demonstrated that ShcC interacts with the protein tyrosine phosphatase STEP, and this interaction may utilize either the ShcC PTB or SH2 domain. ShcC may regulate the activity of STEP, and thus the phosphorylation of the NMDA receptor.



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