Dr. Gail Seabold

Post-doctoral Fellow with Dr. Robert Wenthold Laboratory of Neurochemistry National Institute of Deafness and other Communication Disorders National Institute of Health Bethesda, Maryland seaboldg@nidcd.nih.gov Graduate Education Dr. Johannes Hell, Advisor at UW Madison 1998-2003

Research Interests:

Our lab has identified a new family of adhesion molecules that we have called Synaptic Adhesion-Like Molecules (SALMs). This family of proteins contains domains similar to those found in proteins previously reported to be involved in cell adhesion, neurite outgrowth, and synaptic plasticity. We found that SALMs are expressed at an early stage in the brain and that their expression continues to increase as the brain develops. The identification of this novel family of adhesion-like molecules that may play a role in neurite outgrowth and synapse development is an interesting finding. However, one intriguing aspect of this family of proteins is their association with NMDA receptors.

The association of SALMs with the NMDA receptor was observed by immunoprecipitating the SALMs from rat brain and probing with antibodies to the NMDA receptor. We investigated this further by showing that over-expressing SALM proteins led to a co-clustering of SALM with the NMDA receptor. This interaction appears to occur through the members of the PSD-95 protein family since both SALMs and the NMDA receptor interact with these proteins. However, our studies also revealed a direct interaction between the NMDA receptor and SALMs, which occurs through the extracellular part of these proteins. How this interaction occurs and its physiological significance are currently being investigated, but one possible role is that this interaction stabilizes one or both of these molecules on the cell surface.

Awards:

2006 Fellows Award for Research Excellence, NIH, Bethesda, MD

Publications: Articles on PubMed

• Wang CY, Chang K, Petralia RS, Wang YX, Seabold GK, and Wenthold RJ. (2006). A novel family of adhesion-like molecules that interacts with the NMDA receptor. J Neurosci. 26:2174-83. PDF PMID 16495444
  
  
• Seabold GK, Burette A, Lim IA, Weinberg RJ, and Hell JW. (2003). Interaction of the tyrosine kinase Pyk2 with the N-methyl-D-aspartate receptor complex via the SH3 domains of PSD-95 and SAP102. J Biol Chem. 78:15040-8. PDF PMID 12576483
  
  
• Seabold GK, Luo J, and Miller MW. (1998). Effect of ethanol on neurotrophin-mediated cell survival and receptor expression in cultures of cortical neurons. Dev Brain Res. 108:139-145. PMID 9693792