Structure and Function of the Proline Rich Domain

The central proline-rich domain is the least conserved region within the Ena/VASP proteins. However, all Ena/VASP proteins harbour proline-rich binding sites that confer binding to profilin within the central region (Reinhard et al. 1995; Gertler et al. 1996; Lambrechts et al. 2000). Mena differs most from VASP and EVL within this domain because it contains a highly charged region of unknown function directly after the EVH1 domain (Gertler et al. 1996). Furthermore, different isoforms of Mena are expressed, and the additional exons are found within the central region. Mena has three additional exons, of which the longest is exclusively present in the 140-kDa neuronal Mena isoform (Gertler et al. 1996). Another Mena isoform, Mena(S), is unique among the Ena/VASP proteins by omitting most of the profilin-binding sites (Tani et al. 2003).

The central proline-rich domain of Ena/VASP proteins also harbours binding sites for SH3 and WW domain-containing proteins. It has been shown that EVL can interact with the SH3 domain of Lyn, nSrc, c-Abl, Spectrin, and Tuba (Lambrechts et al. 2000; Rotter et al. 2005; Salazar et al. 2003; Bournier et al. 2006). VASP interacts with the SH3 domain of LASP-1 and Tuba (Salazar et al. 2003; Keicher et al. 2004). An interaction of Mena with the SH3 domains of c-Abl, Tuba, and Src has been identified (Gertler et al. 1996; Salazar et al. 2003). Finally, the WW domain of FE65 can directly interact with proline-rich peptides in the central region of Mena and EVL (Ermekova et al. 1997; Lambrechts et al. 2000).

0 0

Post a comment