Insights into the native function of α-synuclein
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The Department of Biochemistry, Biophysics, and Molecular Biology was founded to give students an understanding of life principles through the understanding of chemical and physical principles. Among these principles are frontiers of biotechnology such as metabolic networking, the structure of hormones and proteins, genomics, and the like.
History
The Department of Biochemistry and Biophysics was founded in 1959, and was administered by the College of Sciences and Humanities (later, College of Liberal Arts & Sciences). In 1979 it became co-administered by the Department of Agriculture (later, College of Agriculture and Life Sciences). In 1998 its name changed to the Department of Biochemistry, Biophysics, and Molecular Biology.
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1959–present
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- Department of Biochemistry and Biophysics (1959–1998)
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- College of Agriculture and Life Sciences (parent college)
- College of Liberal Arts and Sciences (parent college)
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Abstract
For decades α-synuclein has been the focus of research because of its association with Parkinson's disease and other types of dementia. Recently the focus has shifted from attempting to understand the mode of toxicity of α-synuclein aggregates to trying to identify α-synuclein's healthy physiological function. It has been identified that α-synuclein interacts with the SNARE complex and assists in SNARE-mediated membrane fusion. Utilizing two novel single molecule assays we are able to determine how α-synuclein enhances SNARE
activity. α-synuclein has two major domains: one that buries itself in the phospholipid head groups of a membrane and another that binds to the v-SNARE VAMP2. By using both of these domains α-synuclein can tether vesicles more securely to the plasma membrane providing the SNARE complex more time to form properly.