Background:
The dynamics of a cell-cell interface such as tight junctions or adherensjunctions are important in many developmental, physiological and pathological processes. AF-6 (MLLT4: myeloid/lymphoid or mixed-lineage leukemia translocated to 4) is a 1,612 amino acid protein that contains two N-terminal Ras binding domains (RBD) and a GLGF motif, and is implicated in Ras-mediated signaling events occurring at peripheral cell-cell junctions. AF-6 interacts with F-Actin and Profilin in cell-cell junctions, and may modulate Actin modeling near adhesion complexes. Furthermore, AF-6 coordinates junction adhesion molecule (JAM) recruitment to intercellular junctions through a PDZ domain. Developing mice deficient in AF-6 activity display a loss of neuroepithelial polarity, suggesting that AF-6 activity is an important regulator of cell-cell junctions that influence apical/basolateral asymmetry