Figure 7

Outline of POB1/REPS2 and synopsis of its protein interactions. POB1/REPS2 isoform 2 is represented as a line of 521 residues. The EH domain is from 127 to 226; the central proline-rich region is 308–398; the carboxy-terminal part is a coiled-coil. Evidences presented in this work support interactions involving the first proline rich domain 308–365 (PRD1). The SH3 of Amphiphysin II and the carboxy-terminal SH3 of Grb2 specifically bind a peptide centered around arginine 344, while the 14-3-3 family proteins bind the serine 354, if phosphorylated. The proteins recognized by the EH domain of POB1 are: Epsin [5], Nf-kB [9] and Eps15 [28, 4]. The proteins interacting with the distal proline rich domain and the C-terminal domain are RalBP1 (1), and DDEF1/PAG2/ASAP1 whose SH3 domains bind a peptide including P423 and P425 [6]. The phosphorylation of Ser411 by p34 (cdc2) in mitotic phase [29] is reported, the phosphorylation of Ser354 is discussed in this work. The box below shows the consensus sequence for 14-3-3 and SH3 binding in the POB1 human paralogs and mouse orthologs: human REPS1 Q96D71, mouse REPS1 O54916 and mouse REPS2 Q8OXA6. The POB1 sequence coordinates refer to human REPS2 Q8NFH8-2.