Poster Presentations

 

If you or any of your students wish to make poster presentations, please notify Dr. Anthea Stavroulakis, at Kingsborugh Community College, Department of Biological Sciences, 2001 Oriental Boulevard, Brooklyn, NY 11235 (718 368-5095, or e-mail astavroulakis@kbcc.cuny.edu) or Dr. Mary Ortiz, Kingsborough Community College, Department of Biological Sciences, 2001 Oriental Boulevard, Brooklyn, NY 11235 (718 368-5724 or e-mail mortiz@kbcc.cuny.edu).

 

The poster presentations will be displayed on rectangular tables. The presentation must be mounted on a single tri-fold poster board capable of standing on its own. Each presenter will be responsible for setting up and removing his/her own poster presentation. The posters are to be set up by 8 a.m.  
 

Abstracts of the poster presentations should be submitted to the Poster Presentation Co-chairs by mail, preferably on diskette, or e-mail and conform to the following format: The total abstract including title, authors, affiliations, faculty mentors, text and acknowledgements should be typed with an Arial font no smaller than 10 point (title and authors in bold) and sized to fit into a space described by the box below (7.25” X 3.0”). Please follow the form in the sample abstract.

 

Design and Construction of a RET Mutant Expression Vector, Eduardo Areche, and Ramona Kennedy, Montclair State University. Faculty Mentor: Dr. Quinn C. Vega.  

RET is a transmembrane tyrosine kinase activated in response to a liquid. Under normal circumstances, the ligand binds to the extracellular domain leading to activation of the cytoplasmic kinase domain. In specific disease states such as multiple endocrine neoplasma (MEN) 2A and 2B, the receptor is activated in the absence of this ligand leading to thyroid tumors. MEN2A is caused by a mutation in the extracellular domain leading to receptor dimerization and activation. MEN2B is caused by a mutation in the cytoplasmic domain leading to increased activity and altered autophosphorylation. As yet, the sites of autophosphorylation in the MEN2B mutant have not been identified. In order to analyze the phosphorylation pattern and activity of the MEN2B mutant, it would be beneficial to express and purify the protein. In order to rapidly express and purify the RET mutant, a bacterial system will be used. This system consists of a plasmid containing an ampicillin resistance gene and a multi-cloning site located behind the glutathione-S-transferase (GST) gene. Using DNA amplification techniques and other molecular biology tools, this vector will allow us to make a protein consisting of GST and the kinase domain of RET. This fusion protein can then be purified using GST’s affinity for glutathione. By attaching glutathione to beads, the fusion protein can be separated from the column using excess glutathione. Upon purification of the kinase, enzyme activity and function can be further analyzed.

 

 

Sample Abstract