PMID- 10319874
OWN - NLM
STAT- MEDLINE
DCOM- 19990525
LR  - 20071114
IS  - 1061-4036 (Print)
IS  - 1061-4036 (Linking)
VI  - 22
IP  - 1
DP  - 1999 May
TI  - Synphilin-1 associates with alpha-synuclein and promotes the formation of
      cytosolic inclusions.
PG  - 110-4
AB  - Parkinson disease (PD) is a neurodegenerative disease characterized by tremor,
      bradykinesia, rigidity and postural instability. Post-mortem examination shows
      loss of neurons and Lewy bodies, which are cytoplasmic eosinophilic inclusions,
      in the substantia nigra and other brain regions. A few families have PD caused by
      mutations (A53T or A30P) in the gene SNCA (encoding alpha-synuclein).
      Alpha-synuclein is present in Lewy bodies of patients with sporadic PD,
      suggesting that alpha-synuclein may be involved in the pathogenesis of PD. It is 
      unknown how alpha-synuclein contributes to the cellular and biochemical
      mechanisms of PD, and its normal functions and biochemical properties are poorly 
      understood. To determine the protein-interaction partners of alpha-synuclein, we 
      performed a yeast two-hybrid screen. We identified a novel interacting protein,
      which we term synphilin-1 (encoded by the gene SNCAIP). We found that
      alpha-synuclein interacts in vivo with synphilin-1 in neurons. Co-transfection of
      both proteins (but not control proteins) in HEK 293 cells yields cytoplasmic
      eosinophilic inclusions.
FAU - Engelender, S
AU  - Engelender S
AD  - Department of Psychiatry, Johns Hopkins University School of Medicine, Baltimore,
      Maryland 21205, USA.
FAU - Kaminsky, Z
AU  - Kaminsky Z
FAU - Guo, X
AU  - Guo X
FAU - Sharp, A H
AU  - Sharp AH
FAU - Amaravi, R K
AU  - Amaravi RK
FAU - Kleiderlein, J J
AU  - Kleiderlein JJ
FAU - Margolis, R L
AU  - Margolis RL
FAU - Troncoso, J C
AU  - Troncoso JC
FAU - Lanahan, A A
AU  - Lanahan AA
FAU - Worley, P F
AU  - Worley PF
FAU - Dawson, V L
AU  - Dawson VL
FAU - Dawson, T M
AU  - Dawson TM
FAU - Ross, C A
AU  - Ross CA
LA  - eng
SI  - GENBANK/AF076929
GR  - NS16375/NS/NINDS NIH HHS/United States
GR  - NS38377/NS/NINDS NIH HHS/United States
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PT  - Research Support, U.S. Gov't, P.H.S.
PL  - United States
TA  - Nat Genet
JT  - Nature genetics
JID - 9216904
RN  - 0 (Carrier Proteins)
RN  - 0 (Nerve Tissue Proteins)
RN  - 0 (RNA, Messenger)
RN  - 0 (SNCA protein, human)
RN  - 0 (SNCAIP protein, human)
RN  - 0 (Snca protein, rat)
RN  - 0 (Sncaip protein, rat)
RN  - 0 (Synucleins)
RN  - 0 (Tissue Extracts)
RN  - 0 (alpha-Synuclein)
SB  - IM
MH  - Amino Acid Sequence
MH  - Animals
MH  - Brain Chemistry
MH  - Carrier Proteins/genetics/*metabolism
MH  - Cell Line
MH  - Chromosomes, Human, Pair 5/genetics
MH  - Female
MH  - Humans
MH  - Inclusion Bodies/*metabolism
MH  - Lewy Bodies/metabolism
MH  - Male
MH  - Molecular Sequence Data
MH  - Nerve Tissue Proteins/genetics/*metabolism
MH  - Parkinson Disease/genetics/metabolism
MH  - Plasmids/genetics
MH  - Protein Binding
MH  - RNA, Messenger/genetics/metabolism
MH  - Rats
MH  - Saccharomyces cerevisiae/genetics
MH  - Sequence Homology, Amino Acid
MH  - Synucleins
MH  - Tissue Distribution
MH  - Tissue Extracts/metabolism
MH  - Transfection
MH  - alpha-Synuclein
EDAT- 1999/05/13 02:03
MHDA- 2001/03/23 10:01
CRDT- 1999/05/13 02:03
PHST- 1999/05/13 02:03 [pubmed]
PHST- 2001/03/23 10:01 [medline]
PHST- 1999/05/13 02:03 [entrez]
AID - 10.1038/8820 [doi]
PST - ppublish
SO  - Nat Genet. 1999 May;22(1):110-4. doi: 10.1038/8820.