| Description | The zona occuldens proteins (ZO-1, ZO-2 and ZO-3) are a family of tight junction associated proteins that function as cross-linkers, anchoring the TJ strand proteins to the actin-based cytoskeleton [ ]. Each protein contains three PDZ (postsynaptic density, disc-large, ZO-1) domains, a single SH3 (Src Homology-3) domain and a catalytically inactive GK (guanylate kinase) domain, the presence of which identifies them as members of the membrane-associated guanylate kinase (MAGUK) protein family. The signature PDZ-SH3-GuK tandem of MAGUKs may form a structural supramodule with three domains interacting with each other to assemble into an integral structural unit [, ].This entry represents ZO-1, which was first identified as a 220kDa antigen for a monoclonal antibody raised to junction-enriched cell fractions [ ]. The protein shares ~65% overall similarity with ZO-2 and ZO-3 proteins, with highest levels of similarity in the MAGUK and acid domains. The structure of ZO-1 is distinct from the other ZO protein family members in that it contains a ZU5 domain at the C-terminal end of the molecule, although the function of this domain is unknown. Binding and tranfection studies indicate that ZO-1 is capable of associating with ZO-2 and ZO-3 through binding of the second PDZ domains []. | Name | Tight junction protein ZO-1 |
| Short Name | ZO-1 | Type | Family |
Powered by
Have you tried our InterMine mobile apps?
and interoperation is funded by 
