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. 2014 Oct 15;9(10):e109824. doi: 10.1371/journal.pone.0109824

Figure 1. Comparison of the C-termini of rat VGLUT1 and 2.

Figure 1

(A) VGLUT1 and VGLUT2 both contain an acidic dileucine-like internalization motif (underlined) and two lysine residues on either side of a potential PEST ubiquitination domain (+). VGLUT1 contains two PP domains (bold) not found in VGLUT2. VGLUT1, but not VGLUT2, also contains a region of acidic amino acids with a CK2 phosphorylation consensus sequence, S/T-D/E-X-D/E/pS, (italics) containing two serine residues (shaded). In addition, the VGLUT1 acidic domain and PP1 together fit the consensus for a second PEST domain (+). (B) VGLUT1 PP1 contains three sequences that fit the consensus for SH3 protein interaction domains (PXXP) and one for a WW protein interaction domain (PPXY). Starred proline residues are mutated singly to alanine (P531A, P537A, P535A, P539A) to individually disrupt SH3 1, 2, or 3 (PXXP), or WW (PPXY) binding. The mutation P534A + P535A disrupts all three SH3 binding domains (see Fig. 4B).