Similarly, homo-oligomerization regulates the subcellular distribution and signaling capacity of LOUREIRIN-B receptors in the endocytic pathway. These include GABA, leukotriene B, and Toll/interleukin-1 receptors. Critical to understand the effects that membrane protein homo-oligomerization exert on Gentamycin Sulfate proteins is the definition of chemical interactions that hold membrane protein homo-oligomers. Identification of key residues and interfacial domains offers molecular targets to assess the functional role of chemical modifications involved in oligomerization and to predict homo-oligomerization in other membrane proteins. Here we present a new covalent homooligomerization mechanism in a member of the SLC30A family of zinc transporters that depends on redox-regulated covalent tyrosine dimerization. Homo-oligomerization of membrane proteins occurs through non-covalent and covalent interactions, primarily within transmembrane domains. These interactions rely on glycine, leucine or cysteine residues. Among the non-covalent interactions, the most common involve GxxxG and GxxxG-like domains such as those found in glycophorin A, membrane transporters, and receptors. On the other hand, covalent oligomers are mostly mediated by disulfide bonds, like those in cell adhesion molecules and signaling receptors. A far less explored covalent oligomerization mechanism is that dependent on dityrosine bond formation. Dityrosine bonds are present in a limited group of structural proteins of the bacteria cell wall, invertebrate connective tissue, and in proteins of the vertebrate extracellular matrix. Dityrosine bonds have been found in only one membrane protein, the angiotensin II AT2 receptor. Dityrosine bond formation increases with aging, cellular stress, UV and c irradiation and disease. Increased levels of dityrosine modified proteins have been found in lesions such as atheromatous plates and cataracts ; in pathological processes such as acute inflammation and systemic bacterial infection. Recently dityrosine bonds have been associated with a-synuclein fibrillogenesis and Ab amyloid oligomerization. In all these cases dityrosine bonds are thought to represent the cumulative damage of a protein or to regulate protein function by either decreasing the solubility of secreted proteins or increasing oligomer resilience to mechanical stress.