The entry represents the PDZ-binding domain of Harmonin-binding protein USHBP1 (also known as MCC2, mutated in colon cancer-2). USHBP1 has high homology to tumour suppressor MCC1 (mutated in colon cancer-1).MCC2 protein binds the first PDZ domain of AIE-75 (also known as Harmonin) with its C-terminal amino acids -DTFL. A possible role of MCC2 as a tumour suppressor has been put forward. The carboxyl terminus of the predicted protein was DTFL which matched the consensus motif X-S/T-X-phi (phi: hydrophobic amino acid residue) for binding to the PDZ domain of AIE-75 [, ].
This entry includes Harmonin-binding protein USHBP1 also known as MCC2) and colorectal mutant cancer protein known as MCC. MCC has been found to suppresses cell proliferation and the Wnt/b-catenin pathway in colorectal cancer cells [, ]. It may works as a scaffold protein regulating cell movement and able to bind Scrib, beta-catenin and NHERF1/2 []. MCC1 inhibits DNA binding of b-catenin/TCF/LEF transcription factors, and it is involved in cell migration independently of RAC1, CDC42 and p21-activated kinase (PAK) activation [, , ].MCC2 protein binds the first PDZ domain of AIE-75 with its C-terminal amino acids -DTFL. A possible role of MCC2 as a tumour suppressor has been put forward. The carboxyl terminus of the predicted protein was DTFL which matched the consensus motif X-S/T-X-phi (phi: hydrophobic amino acid residue) for binding to the PDZ domain of AIE-75 [, ].
