Epithelial tight junctions perform a barrier role controlling the movement of water, solutes and immune cells through the paracellular pathway as well as defining the polarity of a cell. How tightly these functions are controlled depends on the composition of proteins at the tight junction. Some of the major protein families that form the "backbone" of the barrier are the zonula occludens (ZO) and claudins. MPDZ is a protein that interacts with various members of these families helping to form and regulate the tight junction structure. Reduction in levels of MPDZ at tight junctions for patients with breast cancer was correlated with a poorer outcome.
MPDZ (MUPP-1) is a large protein of 2042 amino acids that contains 13 individual PDZ domains. These domains bind to the C-terminal 4-5 residues of the target protein, localising the proteins to defined regions. The large number of PDZ domains in MPDZ allows the protein to form many connections with several different proteins thus helping to form the large protein scaffold assemblies found at tight junctions. It is believed that alterations in the composition of the tight junction proteins can have significant physiological effects such as the degree of severity of withdrawal symptoms from ethanol and the barbiturate pentobarbital was greater in mice with lower levels of MPDZ expression
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Read more: Proteases Enzyme
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