4.

Structural and functional features of the serine-rich domain of DLC-1. (A). Graphical representation of the predicted secondary structure of the human DLC-1 protein, performed using the FoldIndex program (http://bioportal.weizmann.ac.il/fldbin/findex). The serine-rich region between the SAM and RhoGAP domains is predicted to have a largely unfolded conformation. (B). Features of the serine-rich region. The amino acid sequence of the region between the SAM and RhoGAP domains (residues 79–638) of human DLC-1 is shown, and residues that were found to be phosphorylated in the mouse [51] and rat [49,50] DLC-1 proteins are indicated in yellow. Phosphorylation of Ser549 was presumed, since the equivalent serine in a highly conserved region of mouse DLC-2 was phosphorylated [51]. The tensin-binding site (SIYDNV) and the LD motif (LDDILYHV) are shown in blue.