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<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{Infobox_gene}}
{{PBB_Controls
'''Synphilin-1''' is a [[protein]] that in humans is encoded by the ''SNCAIP'' [[gene]].<ref name="pmid10319874">{{cite journal | vauthors = Engelender S, Kaminsky Z, Guo X, Sharp AH, Amaravi RK, Kleiderlein JJ, Margolis RL, Troncoso JC, Lanahan AA, Worley PF, Dawson VL, Dawson TM, Ross CA | title = Synphilin-1 associates with alpha-synuclein and promotes the formation of cytosolic inclusions | journal = Nat Genet | volume = 22 | issue = 1 | pages = 110–4 | date = May 1999 | pmid = 10319874 | pmc =  | doi = 10.1038/8820 }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: SNCAIP synuclein, alpha interacting protein (synphilin)| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=9627| accessdate = }}</ref> ''SNCAIP'' stands for "synuclein, alpha interacting protein" and can be signified by SNCAP_HUMAN, synphilin 1, synuclein, alpha interacting protein (synphilin), and SYPH1.
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}


<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
== Function ==
{{GNF_Protein_box
| image =
| image_source =
| PDB =
| Name = Synuclein, alpha interacting protein (synphilin)
| HGNCid = 11139
| Symbol = SNCAIP
| AltSymbols =; MGC39814; SYPH1
| OMIM = 603779
| ECnumber = 
| Homologene = 3987
| MGIid = 1915097
| GeneAtlas_image1 = PBB_GE_SNCAIP_219511_s_at_tn.png
| Function = {{GNF_GO|id=GO:0005515 |text = protein binding}}
| Component = {{GNF_GO|id=GO:0005737 |text = cytoplasm}} {{GNF_GO|id=GO:0042734 |text = presynaptic membrane}} {{GNF_GO|id=GO:0043025 |text = cell soma}}
| Process = {{GNF_GO|id=GO:0042417 |text = dopamine metabolic process}} {{GNF_GO|id=GO:0046928 |text = regulation of neurotransmitter secretion}}
| Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 9627
    | Hs_Ensembl = ENSG00000064692
    | Hs_RefseqProtein = NP_005451
    | Hs_RefseqmRNA = NM_005460
    | Hs_GenLoc_db = 
    | Hs_GenLoc_chr = 5
    | Hs_GenLoc_start = 121675719
    | Hs_GenLoc_end = 121827693
    | Hs_Uniprot = Q9Y6H5
    | Mm_EntrezGene = 67847
    | Mm_Ensembl = ENSMUSG00000024534
    | Mm_RefseqmRNA = NM_026408
    | Mm_RefseqProtein = NP_080684
    | Mm_GenLoc_db = 
    | Mm_GenLoc_chr = 18
    | Mm_GenLoc_start = 52893463
    | Mm_GenLoc_end = 53041300
    | Mm_Uniprot = 
  }}
}}
'''Synuclein, alpha interacting protein (synphilin)''', also known as '''SNCAIP''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: SNCAIP synuclein, alpha interacting protein (synphilin)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=9627| accessdate = }}</ref>


<!-- The PBB_Summary template is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
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.<ref name="entrez" />
{{PBB_Summary
| section_title =
| summary_text = 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.<ref name="entrez">{{cite web | title = Entrez Gene: SNCAIP synuclein, alpha interacting protein (synphilin)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=9627| accessdate = }}</ref>
}}


==References==
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.
{{reflist|2}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal  | author=Krüger R |title=The role of synphilin-1 in synaptic function and protein degradation. |journal=Cell Tissue Res. |volume=318 |issue= 1 |pages= 195-9 |year= 2005 |pmid= 15322916 |doi= 10.1007/s00441-004-0953-z }}
*{{cite journal  | author=Engelender S, Kaminsky Z, Guo X, ''et al.'' |title=Synphilin-1 associates with alpha-synuclein and promotes the formation of cytosolic inclusions. |journal=Nat. Genet. |volume=22 |issue= 1 |pages= 110-4 |year= 1999 |pmid= 10319874 |doi= 10.1038/8820 }}
*{{cite journal  | author=Engelender S, Wanner T, Kleiderlein JJ, ''et al.'' |title=Organization of the human synphilin-1 gene, a candidate for Parkinson's disease. |journal=Mamm. Genome |volume=11 |issue= 9 |pages= 763-6 |year= 2000 |pmid= 10967135 |doi=  }}
*{{cite journal  | author=Kawamata H, McLean PJ, Sharma N, Hyman BT |title=Interaction of alpha-synuclein and synphilin-1: effect of Parkinson's disease-associated mutations. |journal=J. Neurochem. |volume=77 |issue= 3 |pages= 929-34 |year= 2001 |pmid= 11331421 |doi=  }}
*{{cite journal  | author=Chung KK, Zhang Y, Lim KL, ''et al.'' |title=Parkin ubiquitinates the alpha-synuclein-interacting protein, synphilin-1: implications for Lewy-body formation in Parkinson disease. |journal=Nat. Med. |volume=7 |issue= 10 |pages= 1144-50 |year= 2001 |pmid= 11590439 |doi= 10.1038/nm1001-1144 }}
*{{cite journal  | author=Ribeiro CS, Carneiro K, Ross CA, ''et al.'' |title=Synphilin-1 is developmentally localized to synaptic terminals, and its association with synaptic vesicles is modulated by alpha-synuclein. |journal=J. Biol. Chem. |volume=277 |issue= 26 |pages= 23927-33 |year= 2002 |pmid= 11956199 |doi= 10.1074/jbc.M201115200 }}
*{{cite journal  | author=O'Farrell C, Pickford F, Vink L, ''et al.'' |title=Sequence conservation between mouse and human synphilin-1. |journal=Neurosci. Lett. |volume=322 |issue= 1 |pages= 9-12 |year= 2002 |pmid= 11958831 |doi=  }}
*{{cite journal  | author=Neystat M, Rzhetskaya M, Kholodilov N, Burke RE |title=Analysis of synphilin-1 and synuclein interactions by yeast two-hybrid beta-galactosidase liquid assay. |journal=Neurosci. Lett. |volume=325 |issue= 2 |pages= 119-23 |year= 2002 |pmid= 12044636 |doi=  }}
*{{cite journal  | author=Junn E, Lee SS, Suhr UT, Mouradian MM |title=Parkin accumulation in aggresomes due to proteasome impairment. |journal=J. Biol. Chem. |volume=277 |issue= 49 |pages= 47870-7 |year= 2003 |pmid= 12364339 |doi= 10.1074/jbc.M203159200 }}
*{{cite journal  | author=Strausberg RL, Feingold EA, Grouse LH, ''et al.'' |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899-903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899 }}
*{{cite journal  | author=Ihara M, Tomimoto H, Kitayama H, ''et al.'' |title=Association of the cytoskeletal GTP-binding protein Sept4/H5 with cytoplasmic inclusions found in Parkinson's disease and other synucleinopathies. |journal=J. Biol. Chem. |volume=278 |issue= 26 |pages= 24095-102 |year= 2003 |pmid= 12695511 |doi= 10.1074/jbc.M301352200 }}
*{{cite journal  | author=Ito T, Niwa J, Hishikawa N, ''et al.'' |title=Dorfin localizes to Lewy bodies and ubiquitylates synphilin-1. |journal=J. Biol. Chem. |volume=278 |issue= 31 |pages= 29106-14 |year= 2003 |pmid= 12750386 |doi= 10.1074/jbc.M302763200 }}
*{{cite journal  | author=Marx FP, Holzmann C, Strauss KM, ''et al.'' |title=Identification and functional characterization of a novel R621C mutation in the synphilin-1 gene in Parkinson's disease. |journal=Hum. Mol. Genet. |volume=12 |issue= 11 |pages= 1223-31 |year= 2004 |pmid= 12761037 |doi=  }}
*{{cite journal  | author=Scherzer CR, Jensen RV, Gullans SR, Feany MB |title=Gene expression changes presage neurodegeneration in a Drosophila model of Parkinson's disease. |journal=Hum. Mol. Genet. |volume=12 |issue= 19 |pages= 2457-66 |year= 2004 |pmid= 12915459 |doi= 10.1093/hmg/ddg265 }}
*{{cite journal  | author=Nagano Y, Yamashita H, Takahashi T, ''et al.'' |title=Siah-1 facilitates ubiquitination and degradation of synphilin-1. |journal=J. Biol. Chem. |volume=278 |issue= 51 |pages= 51504-14 |year= 2004 |pmid= 14506261 |doi= 10.1074/jbc.M306347200 }}
*{{cite journal  | author=Tanaka M, Kim YM, Lee G, ''et al.'' |title=Aggresomes formed by alpha-synuclein and synphilin-1 are cytoprotective. |journal=J. Biol. Chem. |volume=279 |issue= 6 |pages= 4625-31 |year= 2004 |pmid= 14627698 |doi= 10.1074/jbc.M310994200 }}
*{{cite journal  | author=Lee G, Tanaka M, Park K, ''et al.'' |title=Casein kinase II-mediated phosphorylation regulates alpha-synuclein/synphilin-1 interaction and inclusion body formation. |journal=J. Biol. Chem. |volume=279 |issue= 8 |pages= 6834-9 |year= 2004 |pmid= 14645218 |doi= 10.1074/jbc.M312760200 }}
*{{cite journal  | author=Ota T, Suzuki Y, Nishikawa T, ''et al.'' |title=Complete sequencing and characterization of 21,243 full-length human cDNAs. |journal=Nat. Genet. |volume=36 |issue= 1 |pages= 40-5 |year= 2004 |pmid= 14702039 |doi= 10.1038/ng1285 }}
*{{cite journal  | author=Chung KK, Thomas B, Li X, ''et al.'' |title=S-nitrosylation of parkin regulates ubiquitination and compromises parkin's protective function. |journal=Science |volume=304 |issue= 5675 |pages= 1328-31 |year= 2004 |pmid= 15105460 |doi= 10.1126/science.1093891 }}
}}
{{refend}}


{{protein-stub}}
== Interactions ==
{{WikiDoc Sources}}
 
SNCAIP has been shown to [[Protein-protein interaction|interact]] with:
* [[Alpha-synuclein]]<ref name = pmid10319874 /><ref name = pmid12044636>{{cite journal | vauthors = Neystat M, Rzhetskaya M, Kholodilov N, Burke RE | title = Analysis of synphilin-1 and synuclein interactions by yeast two-hybrid beta-galactosidase liquid assay | journal = Neurosci. Lett. | volume = 325 | issue = 2 | pages = 119–23 | date = June 2002 | pmid = 12044636 | doi =  10.1016/s0304-3940(02)00253-7}}</ref><ref name = pmid11742726>{{cite journal | vauthors = Nagano Y, Yamashita H, Nakamura T, Takahashi T, Kondo E, Nakamura S | title = Lack of binding observed between human alpha-synuclein and Bcl-2 protein family | journal = Neurosci. Lett. | volume = 316 | issue = 2 | pages = 103–7 | date = Dec 2001 | pmid = 11742726 | doi =  10.1016/s0304-3940(01)02330-8}}</ref><ref name = pmid11331421>{{cite journal | vauthors = Kawamata H, McLean PJ, Sharma N, Hyman BT | title = Interaction of alpha-synuclein and synphilin-1: effect of Parkinson's disease-associated mutations | journal = J. Neurochem. | volume = 77 | issue = 3 | pages = 929–34 | date = May 2001 | pmid = 11331421 | doi =  10.1046/j.1471-4159.2001.00301.x}}</ref>  and
* [[Parkin (ligase)]].<ref name = pmid11590439>{{cite journal | vauthors = Chung KK, Zhang Y, Lim KL, Tanaka Y, Huang H, Gao J, Ross CA, Dawson VL, Dawson TM | title = Parkin ubiquitinates the alpha-synuclein-interacting protein, synphilin-1: implications for Lewy-body formation in Parkinson disease | journal = Nat. Med. | volume = 7 | issue = 10 | pages = 1144–50 | date = October 2001 | pmid = 11590439 | doi = 10.1038/nm1001-1144 }}</ref>
 
== References ==
{{Reflist}}
 
== Further reading ==
{{Refbegin | 2}}
* {{cite journal | vauthors = Krüger R | title = The role of synphilin-1 in synaptic function and protein degradation | journal = Cell Tissue Res. | volume = 318 | issue = 1 | pages = 195–9 | year = 2005 | pmid = 15322916 | doi = 10.1007/s00441-004-0953-z }}
* {{cite journal | vauthors = Engelender S, Wanner T, Kleiderlein JJ, Wakabayashi K, Tsuji S, Takahashi H, Ashworth R, Margolis RL, Ross CA | title = Organization of the human synphilin-1 gene, a candidate for Parkinson's disease | journal = Mamm. Genome | volume = 11 | issue = 9 | pages = 763–6 | year = 2000 | pmid = 10967135 | doi = 10.1007/s003350010123 }}
* {{cite journal | vauthors = Kawamata H, McLean PJ, Sharma N, Hyman BT | title = Interaction of alpha-synuclein and synphilin-1: effect of Parkinson's disease-associated mutations | journal = J. Neurochem. | volume = 77 | issue = 3 | pages = 929–34 | year = 2001 | pmid = 11331421 | doi = 10.1046/j.1471-4159.2001.00301.x }}
* {{cite journal | vauthors = Chung KK, Zhang Y, Lim KL, Tanaka Y, Huang H, Gao J, Ross CA, Dawson VL, Dawson TM | title = Parkin ubiquitinates the alpha-synuclein-interacting protein, synphilin-1: implications for Lewy-body formation in Parkinson disease | journal = Nat. Med. | volume = 7 | issue = 10 | pages = 1144–50 | year = 2001 | pmid = 11590439 | doi = 10.1038/nm1001-1144 }}
* {{cite journal | vauthors = Ribeiro CS, Carneiro K, Ross CA, Menezes JR, Engelender S | title = Synphilin-1 is developmentally localized to synaptic terminals, and its association with synaptic vesicles is modulated by alpha-synuclein | journal = J. Biol. Chem. | volume = 277 | issue = 26 | pages = 23927–33 | year = 2002 | pmid = 11956199 | doi = 10.1074/jbc.M201115200 }}
* {{cite journal | vauthors = O'Farrell C, Pickford F, Vink L, McGowan E, Cookson MR | title = Sequence conservation between mouse and human synphilin-1 | journal = Neurosci. Lett. | volume = 322 | issue = 1 | pages = 9–12 | year = 2002 | pmid = 11958831 | doi = 10.1016/S0304-3940(02)00068-X }}
* {{cite journal | vauthors = Neystat M, Rzhetskaya M, Kholodilov N, Burke RE | title = Analysis of synphilin-1 and synuclein interactions by yeast two-hybrid beta-galactosidase liquid assay | journal = Neurosci. Lett. | volume = 325 | issue = 2 | pages = 119–23 | year = 2002 | pmid = 12044636 | doi = 10.1016/S0304-3940(02)00253-7 }}
* {{cite journal | vauthors = Junn E, Lee SS, Suhr UT, Mouradian MM | title = Parkin accumulation in aggresomes due to proteasome impairment | journal = J. Biol. Chem. | volume = 277 | issue = 49 | pages = 47870–7 | year = 2003 | pmid = 12364339 | doi = 10.1074/jbc.M203159200 }}
* {{cite journal | vauthors = Ihara M, Tomimoto H, Kitayama H, Morioka Y, Akiguchi I, Shibasaki H, Noda M, Kinoshita M | title = Association of the cytoskeletal GTP-binding protein Sept4/H5 with cytoplasmic inclusions found in Parkinson's disease and other synucleinopathies | journal = J. Biol. Chem. | volume = 278 | issue = 26 | pages = 24095–102 | year = 2003 | pmid = 12695511 | doi = 10.1074/jbc.M301352200 }}
* {{cite journal | vauthors = Ito T, Niwa J, Hishikawa N, Ishigaki S, Doyu M, Sobue G | title = Dorfin localizes to Lewy bodies and ubiquitylates synphilin-1 | journal = J. Biol. Chem. | volume = 278 | issue = 31 | pages = 29106–14 | year = 2003 | pmid = 12750386 | doi = 10.1074/jbc.M302763200 }}
* {{cite journal | vauthors = Marx FP, Holzmann C, Strauss KM, Li L, Eberhardt O, Gerhardt E, Cookson MR, Hernandez D, Farrer MJ, Kachergus J, Engelender S, Ross CA, Berger K, Schöls L, Schulz JB, Riess O, Krüger R | title = Identification and functional characterization of a novel R621C mutation in the synphilin-1 gene in Parkinson's disease | journal = Hum. Mol. Genet. | volume = 12 | issue = 11 | pages = 1223–31 | year = 2004 | pmid = 12761037 | doi = 10.1093/hmg/ddg134 }}
* {{cite journal | vauthors = Scherzer CR, Jensen RV, Gullans SR, Feany MB | title = Gene expression changes presage neurodegeneration in a Drosophila model of Parkinson's disease | journal = Hum. Mol. Genet. | volume = 12 | issue = 19 | pages = 2457–66 | year = 2004 | pmid = 12915459 | doi = 10.1093/hmg/ddg265 }}
* {{cite journal | vauthors = Nagano Y, Yamashita H, Takahashi T, Kishida S, Nakamura T, Iseki E, Hattori N, Mizuno Y, Kikuchi A, Matsumoto M | title = Siah-1 facilitates ubiquitination and degradation of synphilin-1 | journal = J. Biol. Chem. | volume = 278 | issue = 51 | pages = 51504–14 | year = 2004 | pmid = 14506261 | doi = 10.1074/jbc.M306347200 }}
* {{cite journal | vauthors = Tanaka M, Kim YM, Lee G, Junn E, Iwatsubo T, Mouradian MM | title = Aggresomes formed by alpha-synuclein and synphilin-1 are cytoprotective | journal = J. Biol. Chem. | volume = 279 | issue = 6 | pages = 4625–31 | year = 2004 | pmid = 14627698 | doi = 10.1074/jbc.M310994200 }}
* {{cite journal | vauthors = Lee G, Tanaka M, Park K, Lee SS, Kim YM, Junn E, Lee SH, Mouradian MM | title = Casein kinase II-mediated phosphorylation regulates alpha-synuclein/synphilin-1 interaction and inclusion body formation | journal = J. Biol. Chem. | volume = 279 | issue = 8 | pages = 6834–9 | year = 2004 | pmid = 14645218 | doi = 10.1074/jbc.M312760200 }}
* {{cite journal | vauthors = Chung KK, Thomas B, Li X, Pletnikova O, Troncoso JC, Marsh L, Dawson VL, Dawson TM | title = S-nitrosylation of parkin regulates ubiquitination and compromises parkin's protective function | journal = Science | volume = 304 | issue = 5675 | pages = 1328–31 | year = 2004 | pmid = 15105460 | doi = 10.1126/science.1093891 }}
{{Refend}}
 
 
{{Gene-5-stub}}

Latest revision as of 01:57, 27 October 2017

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Identifiers
Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
Entrez

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Ensembl

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UniProt

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RefSeq (mRNA)

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RefSeq (protein)

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Location (UCSC)n/an/a
PubMed searchn/an/a
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View/Edit Human

Synphilin-1 is a protein that in humans is encoded by the SNCAIP gene.[1][2] SNCAIP stands for "synuclein, alpha interacting protein" and can be signified by SNCAP_HUMAN, synphilin 1, synuclein, alpha interacting protein (synphilin), and SYPH1.

Function

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.[2]

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.

Interactions

SNCAIP has been shown to interact with:

References

  1. ↑ 1.0 1.1 Engelender S, Kaminsky Z, Guo X, Sharp AH, Amaravi RK, Kleiderlein JJ, Margolis RL, Troncoso JC, Lanahan AA, Worley PF, Dawson VL, Dawson TM, Ross CA (May 1999). "Synphilin-1 associates with alpha-synuclein and promotes the formation of cytosolic inclusions". Nat Genet. 22 (1): 110–4. doi:10.1038/8820. PMID 10319874.
  2. ↑ 2.0 2.1 "Entrez Gene: SNCAIP synuclein, alpha interacting protein (synphilin)".
  3. ↑ 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. PMID 12044636.
  4. ↑ 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. PMID 11742726.
  5. ↑ Kawamata H, McLean PJ, Sharma N, Hyman BT (May 2001). "Interaction of alpha-synuclein and synphilin-1: effect of Parkinson's disease-associated mutations". J. Neurochem. 77 (3): 929–34. doi:10.1046/j.1471-4159.2001.00301.x. PMID 11331421.
  6. ↑ 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. PMID 11590439.

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. PMID 15322916.
  • 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. PMID 10967135.
  • Kawamata H, McLean PJ, Sharma N, Hyman BT (2001). "Interaction of alpha-synuclein and synphilin-1: effect of Parkinson's disease-associated mutations". J. Neurochem. 77 (3): 929–34. doi:10.1046/j.1471-4159.2001.00301.x. PMID 11331421.
  • Chung KK, Zhang Y, Lim KL, Tanaka Y, Huang H, Gao J, Ross CA, Dawson VL, Dawson TM (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. PMID 11590439.
  • Ribeiro CS, Carneiro K, Ross CA, Menezes JR, Engelender S (2002). "Synphilin-1 is developmentally localized to synaptic terminals, and its association with synaptic vesicles is modulated by alpha-synuclein". J. Biol. Chem. 277 (26): 23927–33. doi:10.1074/jbc.M201115200. PMID 11956199.
  • 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. PMID 11958831.
  • 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. PMID 12044636.
  • Junn E, Lee SS, Suhr UT, Mouradian MM (2003). "Parkin accumulation in aggresomes due to proteasome impairment". J. Biol. Chem. 277 (49): 47870–7. doi:10.1074/jbc.M203159200. PMID 12364339.
  • Ihara M, Tomimoto H, Kitayama H, Morioka Y, Akiguchi I, Shibasaki H, Noda M, Kinoshita M (2003). "Association of the cytoskeletal GTP-binding protein Sept4/H5 with cytoplasmic inclusions found in Parkinson's disease and other synucleinopathies". J. Biol. Chem. 278 (26): 24095–102. doi:10.1074/jbc.M301352200. PMID 12695511.
  • Ito T, Niwa J, Hishikawa N, Ishigaki S, Doyu M, Sobue G (2003). "Dorfin localizes to Lewy bodies and ubiquitylates synphilin-1". J. Biol. Chem. 278 (31): 29106–14. doi:10.1074/jbc.M302763200. PMID 12750386.
  • Marx FP, Holzmann C, Strauss KM, Li L, Eberhardt O, Gerhardt E, Cookson MR, Hernandez D, Farrer MJ, Kachergus J, Engelender S, Ross CA, Berger K, Schöls L, Schulz JB, Riess O, Krüger R (2004). "Identification and functional characterization of a novel R621C mutation in the synphilin-1 gene in Parkinson's disease". Hum. Mol. Genet. 12 (11): 1223–31. doi:10.1093/hmg/ddg134. PMID 12761037.
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