Fig. 1

Domain structures of YAP and TAZ. YAP is a 65-kDa protein containing a proline-rich region (P-rich) in the N-terminal region and a PDZ-binding motif (PDZ-BM) in the C-terminal region that are separated by two WW domains, a TEAD binding domain, a Src homology domain 3 binding motif (SH3-BM), and a coiled–coil domain (CC) within the transactivation domain (TAD). There are 8 isoforms of YAP exist which differ by loss of one WW domain and alterations in TAD. TAZ, a 43-kDa paralog of YAP, has similar domain organization but lacks the proline-rich region, the SH3-BM and one WW domain. YAP S127 and TAZ S89 are the main phosphorylation targets of LATS1/2. Upon phosphorylation YAP/TAZ binds with 14-3-3 and thus are sequestered in the cytoplasm