Edward Benz, Jr.

The Benz laboratory focuses on the molecular pathology and physiology of red cell development, the molecular basis of inherited hemolytic anemias, and the use of the red cell homeostatic system as a model to study gene regulation differentiation and growth control in other tissues. 

During the past five years, Benz and colleagues have focused on the structure, function, gene regulation, and molecular pathology of protein 4.1. This cytoskeletal protein, originally described in the red cell, forms a ternary complex with spectrin actin, and attaches the spectrin latticework to membranes by binding to the cytoplasmic domains of key transmembrane proteins. Defects in this protein are associated with hereditary erythrocytosis. 

The laboratory has shown that many isoforms of protein 4.1 arise from a single protein 4.1R gene by tissue-specific and stage-specific alternative mRNA splicing pathways, a number of which they have characterized. The group has identified at least three several key target sequence areas motifs and one putative has implicated and characterized at least three splicing factors involved governing the in tissue-specific regulation of red cell isoforms during erythroid differentiation. 

In addition, structure function studies of p4.1R isoforms produced in other cell lineages have shown that they play key roles in mitosis, cell-cell junctions and muscle costameres. For example, disruption of p4.1R expression alters the topology of the mitotic spindle and promotes the development of aneuploidy.