Retention of p63 in an ER-Golgi intermediate compartment depends on the presence of all three of its domains and on its ability to form oligomers

(R 7, C -s, K ~°, G It , K 2~, and G 22) by alanines (MP4) resulted in transport of the mutant protein to the plasma membrane, indicating the importance of the corresponding amino acids for correct localization of p63. Interestingly, changing either the positively charged residues or the glycines alone (MP2, MP3) did not affect retention of p63. Further, the dements required for retention appear to be at least partly redundant as revealed by the analysis of the overlapping alanine scan of A24-101, a similar scan of AI6-101, and the cytoplasmic tail deletion mutants.