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Gene Review

SNCAIP  -  synuclein, alpha interacting protein

Homo sapiens

Synonyms: Alpha-synuclein-interacting protein, SYPH1, Sph1, Synphilin-1
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Disease relevance of SNCAIP


Psychiatry related information on SNCAIP


High impact information on SNCAIP


Chemical compound and disease context of SNCAIP

  • The mechanism by which alpha-syn induces neuronal cell toxicity may invoke multiple pathways, such as aggregation or interaction with other proteins and molecules, including synphilin-1, chaperone 14-3-3 protein, and dopamine itself [9].

Biological context of SNCAIP


Anatomical context of SNCAIP


Associations of SNCAIP with chemical compounds

  • These eosinophilic inclusions share many characteristics with Lewy bodies, including a core and halo organization, immunoreactivity to ubiquitin, alpha-synuclein, synphilin-1, Parkin, molecular chaperones, and proteasome subunit as well as staining of some with thioflavin S [15].
  • Additionally, we show sensitivity of both endogenous synphilin-1 and parkin to proteolytic dysfunction and their co-localization in aggresomes formed in response to the proteasome inhibitor MG-132 [16].
  • This unique activity of parkin mediates a non-classical, lysine (K) 63-linked ubiquitin multichain assembly on synphilin-1 that is distinct from the classical, degradation-associated, K48-linked ubiquitination [17].
  • The C-terminus of Synphilin-1 was found to selectively bind to acidic phospholipids, including phosphatidic acid, phosphatidylserine, and phosphatidylglycerol, but not to naturally charged phospholipids [18].
  • Co-transfection of synphilin and the central (NAC) region of alpha-syn in HEH293 cells resulted in synuclein inclusions [19].

Physical interactions of SNCAIP


Enzymatic interactions of SNCAIP


Co-localisations of SNCAIP


Regulatory relationships of SNCAIP


Other interactions of SNCAIP


Analytical, diagnostic and therapeutic context of SNCAIP


  1. Organization of the human synphilin-1 gene, a candidate for Parkinson's disease. Engelender, S., Wanner, T., Kleiderlein, J.J., Wakabayashi, K., Tsuji, S., Takahashi, H., Ashworth, R., Margolis, R.L., Ross, C.A. Mamm. Genome (2000) [Pubmed]
  2. Aggresomes formed by alpha-synuclein and synphilin-1 are cytoprotective. Tanaka, M., Kim, Y.M., Lee, G., Junn, E., Iwatsubo, T., Mouradian, M.M. J. Biol. Chem. (2004) [Pubmed]
  3. Multiple system atrophy/progressive supranuclear palsy: alpha-Synuclein, synphilin, tau, and APOE. Morris, H.R., Vaughan, J.R., Datta, S.R., Bandopadhyay, R., Rohan De Silva, H.A., Schrag, A., Cairns, N.J., Burn, D., Nath, U., Lantos, P.L., Daniel, S., Lees, A.J., Quinn, N.P., Wood, N.W. Neurology (2000) [Pubmed]
  4. Immunocytochemical localization of synphilin-1, an alpha-synuclein-associated protein, in neurodegenerative disorders. Wakabayashi, K., Engelender, S., Tanaka, Y., Yoshimoto, M., Mori, F., Tsuji, S., Ross, C.A., Takahashi, H. Acta Neuropathol. (2002) [Pubmed]
  5. Immunohistochemical study of synphilin-1 in brains of patients with dementia with Lewy bodies - synphilin-1 is non-specifically implicated in the formation of different neuronal cytoskeletal inclusions. Iseki, E., Takayama, N., Furukawa, Y., Marui, W., Nakai, T., Miura, S., Uéda, K., Kosaka, K. Neurosci. Lett. (2002) [Pubmed]
  6. Parkin ubiquitinates the alpha-synuclein-interacting protein, synphilin-1: implications for Lewy-body formation in Parkinson disease. Chung, K.K., Zhang, Y., Lim, K.L., Tanaka, Y., Huang, H., Gao, J., Ross, C.A., Dawson, V.L., Dawson, T.M. Nat. Med. (2001) [Pubmed]
  7. Synphilin-1A: an aggregation-prone isoform of synphilin-1 that causes neuronal death and is present in aggregates from alpha-synucleinopathy patients. Eyal, A., Szargel, R., Avraham, E., Liani, E., Haskin, J., Rott, R., Engelender, S. Proc. Natl. Acad. Sci. U.S.A. (2006) [Pubmed]
  8. Ubiquitylation of synphilin-1 and alpha-synuclein by SIAH and its presence in cellular inclusions and Lewy bodies imply a role in Parkinson's disease. Liani, E., Eyal, A., Avraham, E., Shemer, R., Szargel, R., Berg, D., Bornemann, A., Riess, O., Ross, C.A., Rott, R., Engelender, S. Proc. Natl. Acad. Sci. U.S.A. (2004) [Pubmed]
  9. Alpha-synuclein and Parkinson's disease. Recchia, A., Debetto, P., Negro, A., Guidolin, D., Skaper, S.D., Giusti, P. FASEB J. (2004) [Pubmed]
  10. Case-control study of the alpha-synuclein interacting protein gene and Parkinson's disease. Maraganore, D.M., Farrer, M.J., Lesnick, T.G., de Andrade, M., Bower, J.H., Hernandez, D., Hardy, J.A., Rocca, W.A. Mov. Disord. (2003) [Pubmed]
  11. Identification and functional characterization of a novel R621C mutation in the synphilin-1 gene in Parkinson's disease. Marx, F.P., Holzmann, C., Strauss, K.M., Li, L., Eberhardt, O., Gerhardt, E., Cookson, M.R., Hernandez, D., Farrer, M.J., Kachergus, J., Engelender, S., Ross, C.A., Berger, K., Schöls, L., Schulz, J.B., Riess, O., Krüger, R. Hum. Mol. Genet. (2003) [Pubmed]
  12. Casein kinase II-mediated phosphorylation regulates alpha-synuclein/synphilin-1 interaction and inclusion body formation. Lee, G., Tanaka, M., Park, K., Lee, S.S., Kim, Y.M., Junn, E., Lee, S.H., Mouradian, M.M. J. Biol. Chem. (2004) [Pubmed]
  13. Siah-1 facilitates ubiquitination and degradation of synphilin-1. Nagano, Y., Yamashita, H., Takahashi, T., Kishida, S., Nakamura, T., Iseki, E., Hattori, N., Mizuno, Y., Kikuchi, A., Matsumoto, M. J. Biol. Chem. (2003) [Pubmed]
  14. Synphilin-1 is developmentally localized to synaptic terminals, and its association with synaptic vesicles is modulated by alpha-synuclein. Ribeiro, C.S., Carneiro, K., Ross, C.A., Menezes, J.R., Engelender, S. J. Biol. Chem. (2002) [Pubmed]
  15. Parkin accumulation in aggresomes due to proteasome impairment. Junn, E., Lee, S.S., Suhr, U.T., Mouradian, M.M. J. Biol. Chem. (2002) [Pubmed]
  16. Synphilin-1 and parkin show overlapping expression patterns in human brain and form aggresomes in response to proteasomal inhibition. Bandopadhyay, R., Kingsbury, A.E., Muqit, M.M., Harvey, K., Reid, A.R., Kilford, L., Engelender, S., Schlossmacher, M.G., Wood, N.W., Latchman, D.S., Harvey, R.J., Lees, A.J. Neurobiol. Dis. (2005) [Pubmed]
  17. Parkin-mediated lysine 63-linked polyubiquitination: a link to protein inclusions formation in Parkinson's and other conformational diseases? Lim, K.L., Dawson, V.L., Dawson, T.M. Neurobiol. Aging (2006) [Pubmed]
  18. Interactions of Synphilin-1 with phospholipids and lipid membranes. Takahashi, T., Yamashita, H., Nagano, Y., Nakamura, T., Kohriyama, T., Matsumoto, M. FEBS Lett. (2006) [Pubmed]
  19. Synphilin in normal human brains and in synucleinopathies: studies with new antibodies. Murray, I.J., Medford, M.A., Guan, H.P., Rueter, S.M., Trojanowski, J.Q., Lee, V.M. Acta Neuropathol. (2003) [Pubmed]
  20. Lack of binding observed between human alpha-synuclein and Bcl-2 protein family. Nagano, Y., Yamashita, H., Nakamura, T., Takahashi, T., Kondo, E., Nakamura, S. Neurosci. Lett. (2001) [Pubmed]
  21. Dorfin localizes to Lewy bodies and ubiquitylates synphilin-1. Ito, T., Niwa, J., Hishikawa, N., Ishigaki, S., Doyu, M., Sobue, G. J. Biol. Chem. (2003) [Pubmed]
  22. Glycogen synthase kinase 3beta modulates synphilin-1 ubiquitylation and cellular inclusion formation by SIAH: implications for proteasomal function and Lewy body formation. Avraham, E., Szargel, R., Eyal, A., Rott, R., Engelender, S. J. Biol. Chem. (2005) [Pubmed]
  23. NUB1 suppresses the formation of Lewy body-like inclusions by proteasomal degradation of synphilin-1. Tanji, K., Tanaka, T., Mori, F., Kito, K., Takahashi, H., Wakabayashi, K., Kamitani, T. Am. J. Pathol. (2006) [Pubmed]
  24. The role of synphilin-1 in synaptic function and protein degradation. Krüger, R. Cell Tissue Res. (2004) [Pubmed]
  25. Synphilin-1 degradation by the ubiquitin-proteasome pathway and effects on cell survival. Lee, G., Junn, E., Tanaka, M., Kim, Y.M., Mouradian, M.M. J. Neurochem. (2002) [Pubmed]
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