Synaptojanin 1 Mutation in Parkinson’s Disease Brings Further Insight into the Neuropathological Mechanisms

Figure 1

Functional and interaction domains of the two major isoforms of SYNJ1. The 145 kDa (top) and the 170 kDa (bottom) SYNJ1 isoforms harbor two functional inositol phosphatase domains, an N-terminal Sac1 domain and a more central 5′-phosphatase domain. Several protein-protein interaction domains are found in the C-terminal part of the proteins: one or two PRD domains, AP2 binding motifs (WxxF, FxDxF, and DxF, in pink), and Eps15 binding motifs (NPF: asparagine-proline-phenylalanine, in blue). The homozygous mutation Arg258Gln, found in Parkinson’s disease patients, is indicated in red. Numbers indicate the amino acid positions along the proteins. Sac1: suppressor of actin1; PRD: proline-rich domain; AP2: adaptor protein complex 2; Eps15: epidermal growth factor receptor pathway substrate 15.