2KXR
ZO1 ZU5 domain MC/AA mutation
Summary for 2KXR
Entry DOI | 10.2210/pdb2kxr/pdb |
Related | 2KXS |
Descriptor | Tight junction protein ZO-1 (1 entity in total) |
Functional Keywords | beta-barrel, protein binding |
Biological source | Homo sapiens (human) |
Cellular location | Cell membrane; Peripheral membrane protein; Cytoplasmic side: Q07157 |
Total number of polymer chains | 1 |
Total formula weight | 12687.63 |
Authors | |
Primary citation | Huo, L.,Wen, W.,Wang, R.,Kam, C.,Xia, J.,Feng, W.,Zhang, M. Cdc42-dependent formation of the ZO-1/MRCKb complex at the leading edge controls cell migration Embo J., 30:665-678, 2011 Cited by PubMed Abstract: Zonula occludens (ZO)-1 is a multi-domain scaffold protein known to have critical roles in the establishment of cell-cell adhesions and the maintenance of stable tissue structures through the targeting, anchoring, and clustering of transmembrane adhesion molecules and cytoskeletal proteins. Here, we report that ZO-1 directly binds to MRCKβ, a Cdc42 effector kinase that modulates cell protrusion and migration, at the leading edge of migrating cells. Structural studies reveal that the binding of a β hairpin from GRINL1A converts ZO-1 ZU5 into a complete ZU5-fold. A similar interaction mode is likely to occur between ZO-1 ZU5 and MRCKβ. The interaction between ZO-1 and MRCKβ requires the kinase to be primed by Cdc42 due to the closed conformation of the kinase. Formation of the ZO-1/MRCKβ complex enriches the kinase at the lamellae of migrating cells. Disruption of the ZO-1/MRCKβ complex inhibits MRCKβ-mediated cell migration. These results demonstrate that ZO-1, a classical scaffold protein with accepted roles in maintaining cell-cell adhesions in stable tissues, also has an active role in cell migration during processes such as tissue development and remodelling. PubMed: 21240187DOI: 10.1038/emboj.2010.353 PDB entries with the same primary citation |
Experimental method | SOLUTION NMR |
Structure validation
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