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Chaperone-like activity of synucleins
J M Souza1, B I Giasson, V M Lee
1Stokes Research Institute, Children's Hospital of Philadelphia, Department of Biochemistry and Biophysics, 416D Abramson Center, 34th St. and Civic Center Blvd, The University of Pennsylvania Medical Center, Philadelphia, 19104, USA.
Abstract:
Synucleins are a family of small proteins that are predominantly expressed in neurons. The functions of the synucleins are not entirely understood, but they have been implicated in the pathogenesis of several neurodegenerative diseases. Our data show that alpha-, beta- or gamma-synuclein suppresses the aggregation of thermally denatured alcohol dehydrogenase and chemically denatured insulin. The A53T but not the A30P mutant alpha-synuclein was able to inhibit the aggregation of insulin and the chaperone-like activity of alpha-synuclein was lost upon removal of its C-terminal residues 98-140. These results demonstrate that synucleins with the exception of the A30P mutant possess chaperone-like activity.