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Volume 8, Issue 6 (Suppl)
J Bioremediat Biodegrad, an open access journal
ISSN:2155-6199
Biopolymers & Bioplastics 2017
October 19-20, 2017
October 19-20, 2017 San Francisco, USA
7
th
International Conference and Exhibition on
Biopolymers and Bioplastics
Synucleins form oligomers and induce oligomerization of other proteins
Andrei Surguchov
Kansas University Medical Center, USA
Statement of the problem:
Synucleins belong to a family of small naturally unfolded or intrinsically unstructured proteins consisting
of three members: alpha-, beta and gamma-synuclein. Aggregation of alpha-synuclein is associated with Parkinson’s disease and
other neurodegenerative disorders. The susceptibility to the formation of protein aggregates depends on cooperative conformational
changes which may contribute to the kinetic control of fibrillization with transitions between alpha-helical and beta-sheet secondary
structure. The protein aggregates which may be formed under
in vitro
and
in vivo
conditions exhibit significant variations in their
structure and function. Interaction of synucleins with other proteins promotes their oligomerization and affect their dynamics.
Findings:
Alpha-synuclein binds tomicrotubules and tubulin tetramer inducingmicrotubule nucleation and growth rate thus affecting
microtubule dynamics. Alpha-synuclein also affect superoxide dismutase 1 and Tau oligomerization and actin dynamics. Gamma-
synuclein can affect microtubule properties and act as a functional microtubule associated protein. We found that gamma-synuclein
after oxidation of Met-38 acts as anti-chaperone, which is able to enhance alpha-synuclein aggregation and form heterologous
complexes containing both proteins. We identified specific post-translational modifications altering synuclein’s susceptibility to
aggregation. We also found that γ-synuclein affects the formation of actin–cofilin rods 11.2 ± 1.4 μm in length.
Significance:
Such cross-seeding effects of intrinsically unstructured proteins play an important role in the pathogenesis of
neurodegenerative diseases.
asurguchov@kumc.eduJ Bioremediat Biodegrad 2017, 8:6 (Suppl)
DOI: 10.4172/2155-6199-C1-012