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. Author manuscript; available in PMC: 2010 Jul 2.
Published in final edited form as: Front Biosci. 2009 Jan 1;14:1414–1432. doi: 10.2741/3316

Figure 4.

Figure 4

A schematic overview of the DLG-1/AJM-1 complex. This complex, consisting of DLG-1/Discs large and its binding partner, AJM-1, is basal to the cadherin-catenin complex, but is required to stabilize the electron density associated with apical junctions (6, 12, 18). LET-413 targets the DLG-1/AJM-1 complex to apical junctions, and while it may also be present at apical junctions, its localization extends far more basally (18, 19, 93). DLG-1, specifically its L27 domain, is required for efficient spreading of AJM-1 along cell junctions (85). Experiments suggest that the DLG-1/AJM-1 complex acts synergistically with the cadherin-catenin complex to regulate cell adhesion (12, 18). This modulation of cell adhesion presumably involves an unidentified transmembrane protein with which the DLG-1/AJM-1 complex physically interacts. One such protein could be the claudin CLC-1, with which AJM-1 colocalizes in the pharynx (105).