Impaired degradation of mutant α-synuclein by chaperone-mediated autophagy

Science

Volumn 305, Issue 5688, 2004, Pages 1292-1295

  Cuervo, Ana Maria ^a   Stafanis, Leonidas ^b,c   Fredenburg, Ross ^d   Lansbury, Peter T ^d   Sulzer, David ^e  

^a ALBERT EINSTEIN COLLEGE OF MEDICINE   (United States)

^b Found Biomed Res Acad Athens   (Greece)

^c Och Spine at New York Presbyterian Hospitals   (United States)

^d BRIGHAM AND WOMEN S HOSPITAL   (United States)

^e NEW YORK STATE PSYCHIATRIC INSTITUTE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

DEGRADATION; MEMBRANES; PATHOLOGY; PROTEINS; SUBSTRATES;

Α-SYNUCLEIN DEGRADATION; LYSOSOMERS; MUTANTS; PATHOGENESIS;

DISEASES;

ALPHA SYNUCLEIN; CHAPERONE; MUTANT PROTEIN;

MEDICINE;

ARTICLE; AUTOPHAGY; CELL INCLUSION; CONTROLLED STUDY; LEWY BODY; LYSOSOME; PARKINSON DISEASE; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN DEGRADATION; PROTEIN TRANSPORT;

ALPHA-SYNUCLEIN; AMINO ACID MOTIFS; ANIMALS; ANTIGENS, CD; AUTOPHAGY; CELLS, CULTURED; GLYCERALDEHYDE-3-PHOSPHATE DEHYDROGENASES; HALF-LIFE; INTRACELLULAR MEMBRANES; LYSOSOME-ASSOCIATED MEMBRANE GLYCOPROTEINS; LYSOSOMES; MALE; MICE; MOLECULAR CHAPERONES; MUTATION; NERVE TISSUE PROTEINS; NEURONS; PC12 CELLS; PROTEIN BINDING; PROTEIN TRANSPORT; RATS; RATS, WISTAR; SYNUCLEINS;

EID: 4344659685     PISSN: 00368075     EISSN: None     Source Type: Journal    
DOI: 10.1126/science.1101738     Document Type: Article

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30. We are very grateful to B. Giasson and V. Lee for providing us with a human-specific monoclonal antibody to α-synuclein (Syn 211) and to Q. Wang and A. Massey for technical assistance. This work was supported by the NIH/National Institute on Aging grant AG021904 (A.M.C), two National Institute of Neurological Disorders and Stroke Udall Center grants (D.S. and P.L), the Parkinson's Disease Foundation, the Lowenstein Foundation (L.S. and D.S.), the Matheson Foundation (L.S.), a Huntington's Disease Society of America Grant (D.S. and A-M.C.), and the Howard Hughes Medical Institute (A.M.C.). Molecular interaction data have been deposited in the Biomolecular Interaction Network Database with accession code 151734.