Network motif comparison rationalizes Sec1/Munc18-SNARE regulation mechanism in exocytosis
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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.
Dates of Existence
1959–present
Historical Names
- Department of Biochemistry and Biophysics (1959–1998)
Related Units
- College of Agriculture and Life Sciences (parent college)
- College of Liberal Arts and Sciences (parent college)
The Department of Genetics, Development, and Cell Biology seeks to teach subcellular and cellular processes, genome dynamics, cell structure and function, and molecular mechanisms of development, in so doing offering a Major in Biology and a Major in Genetics.
History
The Department of Genetics, Development, and Cell Biology was founded in 2005.
Related Units
- College of Agriculture and Life Sciences (parent college)
- College of Liberal Arts and Sciences (parent college)
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Abstract
Background
Network motifs, recurring subnetwork patterns, provide significant insight into the biological networks which are believed to govern cellular processes.
Methods
We present a comparative network motif experimental approach, which helps to explain complex biological phenomena and increases the understanding of biological functions at the molecular level by exploring evolutionary design principles of network motifs.
Results
Using this framework to analyze the SM (Sec1/Munc18)-SNARE (N-ethylmaleimide-sensitive factor activating protein receptor) system in exocytic membrane fusion in yeast and neurons, we find that the SM-SNARE network motifs of yeast and neurons show distinct dynamical behaviors. We identify the closed binding mode of neuronal SM (Munc18-1) and SNARE (syntaxin-1) as the key factor leading to mechanistic divergence of membrane fusion systems in yeast and neurons. We also predict that it underlies the conflicting observations in SM overexpression experiments. Furthermore, hypothesis-driven lipid mixing assays validated the prediction.
Conclusion
Therefore this study provides a new method to solve the discrepancies and to generalize the functional role of SM proteins.
Comments
This article is from BMC Systems Biology 6 (2012): 19, doi:10.1186/1752-0509-6-19, Posted with permission.