Mediation of Vesicular Fusion by SNARE Proteins during Macroautophagy
The Moeller SMART Team in conjunction with Dr. JiaJie Diao at the University of Cincinnati Medical College and MSOE Center for Biomolecular Modeling used 3‐D modeling and printing technology to study the role of Soluble NSF Attachment Protein Receptor (SNARE) proteins in macroautophagy, a process th...
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| Published in: | The FASEB journal Vol. 33; no. S1; p. lb322 |
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| Main Authors: | , , , , , , , , , , , , , , , |
| Format: | Journal Article |
| Language: | English |
| Published: |
The Federation of American Societies for Experimental Biology
01-04-2019
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| Online Access: | Get full text |
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| Summary: | The Moeller SMART Team in conjunction with Dr. JiaJie Diao at the University of Cincinnati Medical College and MSOE Center for Biomolecular Modeling used 3‐D modeling and printing technology to study the role of Soluble NSF Attachment Protein Receptor (SNARE) proteins in macroautophagy, a process that recycles damaged organelles, proteins, and microbes in the cell. It begins with the formation and maturation of an autophagosome. The process ends with the fusion of a fully matured autophagosome to a lysosome membrane, which is mediated by SNARE proteins. Vesicular fusion is initiated by the formation of a tetrameric alpha‐helix complex that is formed through the binding of three helical SNARE proteins. One of these SNARE proteins, VAMP8, is located on lysosomes and the other two, syntaxin17 and SNAP‐29, are located on the membrane of autophagosomes. The helices of these proteins coil tightly in the alpha‐helix complex which provides the energy for fusion. To reset the conformation of SNARE proteins, N‐Ethylmaleimide‐Sensitive Factor (NSF) proteins use ATP and water to recycle SNAREs. Alpha‐SNAP, an ATPase, which helps to facilitate this process, returns SNARE to its original high energy state. If fusion is unable to occur in autophagy, the cell accumulates autophagosomes, causing lysosome storage diseases such as Parkinson's and Alzheimer's disease. By 3‐D printing the coiled alpha‐helix complex, our SMART team intends to describe this crucial element of membrane fusion and the disorders associated with macroautophagy.
This is from the Experimental Biology 2019 Meeting. There is no full text article associated with this published in The FASEB Journal. |
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| ISSN: | 0892-6638 1530-6860 |
| DOI: | 10.1096/fasebj.2019.33.1_supplement.lb322 |