The connexin family of proteins form hexameric complexes called “connexons” that facilitate movement of low molecular weight proteins between cells via gap junctions (1). Connexin proteins share a common topology of 4 transmembrane alpha-helical domains, two extracellular loops, a cytoplasmic loop, and cytoplasmic N- and C-termini (2). Many of the key functional differences arise from specific amino-acid substitutions in the most highly conserved domains, the transmembrane and extracellular regions (2). Each of the approximately 20 connexin isoforms produces channels with distinct permeabilities and electrical and chemical sensitivities; therefore, one connexin usually cannot fully substitute for another (2). Consequently, a wide variety of malignant phenotypes associate with decreased connexin expression and gap junction communication, dependent on the particular connexin that is effected (3, 2). For instance, deletion of the gene encoding connexin 50, normally expressed in the lens, produces cataracts, though not as severe as with deletion of connexin 46 (4).