Synphilin-1 is a protein that in humans is encoded by the SNCAIPgene.[5][6]SNCAIP stands for "synuclein, alpha interacting protein" and can be signified by SNCAP_HUMAN, synphilin 1, synuclein, alpha interacting protein (synphilin), and SYPH1.
This gene encodes a protein containing several protein-protein interaction domains, including ankyrin-like repeats, a coiled-coil domain, and an ATP/GTP-binding motif. The encoded protein interacts with alpha-synuclein in neuronal tissue and may play a role in the formation of cytoplasmic inclusions and neurodegeneration. A mutation in this gene has been associated with Parkinson's disease. Alternatively spliced transcript variants encoding different isoforms of this gene have been described, but their full-length nature has yet to be determined.[6]
The SNCAIP gene provides instructions for making a protein called synphilin-1 and a slightly different version of this protein called synphilin-1A. These proteins are produced in the brain. They are usually located in specialized structures called presynaptic terminals, found at the tips of nerve cells. In nerve cells, synphilin-1 and synphilin-1A interact with another protein called alpha-synuclein. The functions of synphilin-1 and synphilin-1A, however, are unknown.
^Neystat M, Rzhetskaya M, Kholodilov N, Burke RE (June 2002). "Analysis of synphilin-1 and synuclein interactions by yeast two-hybrid beta-galactosidase liquid assay". Neurosci. Lett. 325 (2): 119–23. doi:10.1016/s0304-3940(02)00253-7. PMID12044636. S2CID11517781.
^Nagano Y, Yamashita H, Nakamura T, Takahashi T, Kondo E, Nakamura S (Dec 2001). "Lack of binding observed between human alpha-synuclein and Bcl-2 protein family". Neurosci. Lett. 316 (2): 103–7. doi:10.1016/s0304-3940(01)02330-8. PMID11742726. S2CID54363210.
^Chung KK, Zhang Y, Lim KL, Tanaka Y, Huang H, Gao J, Ross CA, Dawson VL, Dawson TM (October 2001). "Parkin ubiquitinates the alpha-synuclein-interacting protein, synphilin-1: implications for Lewy-body formation in Parkinson disease". Nat. Med. 7 (10): 1144–50. doi:10.1038/nm1001-1144. PMID11590439. S2CID12487644.
Further reading[]
Krüger R (2005). "The role of synphilin-1 in synaptic function and protein degradation". Cell Tissue Res. 318 (1): 195–9. doi:10.1007/s00441-004-0953-z. PMID15322916. S2CID12186058.
Engelender S, Wanner T, Kleiderlein JJ, Wakabayashi K, Tsuji S, Takahashi H, Ashworth R, Margolis RL, Ross CA (2000). "Organization of the human synphilin-1 gene, a candidate for Parkinson's disease". Mamm. Genome. 11 (9): 763–6. doi:10.1007/s003350010123. PMID10967135. S2CID22420090.
O'Farrell C, Pickford F, Vink L, McGowan E, Cookson MR (2002). "Sequence conservation between mouse and human synphilin-1". Neurosci. Lett. 322 (1): 9–12. doi:10.1016/S0304-3940(02)00068-X. PMID11958831. S2CID9654263.
Neystat M, Rzhetskaya M, Kholodilov N, Burke RE (2002). "Analysis of synphilin-1 and synuclein interactions by yeast two-hybrid beta-galactosidase liquid assay". Neurosci. Lett. 325 (2): 119–23. doi:10.1016/S0304-3940(02)00253-7. PMID12044636. S2CID11517781.