SNARE-ing the structures of Sec1/Munc18 proteins

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Date
2014-12-01
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Elsevier BV
Abstract
Membrane fusion is essential for cellular transport in eukaryotes. Abnormalities contribute to a wide range of diseases including diabetes and neurological disorders. A key regulator of SNARE-mediated membrane fusion is the Sec1/Munc18 (SM) protein family. Universal structural features of SM proteins have been identified that affect the way these interact with their partner Syntaxin SNARE proteins. Whilst the molecular basis for SM-regulated SNARE complex formation has been extensively studied, it remains poorly understood. Recent crystal structures of SM proteins alone or in complex have provided new insight. Here we examine the available structural information on SM proteins for clues to how these enigmatic proteins might regulate SNARE complex assembly and membrane fusion. © 2014, Elsevier Ltd.
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Keywords
Membranes, Chromosomal aberrations, Diabetes mellitus, Proteins, Diseases, Molecules
Citation
Archbold, J. K., Whitten, A. E., Hu, S.-H., Collins, B. M., & Martin, J. L. (2014). SNARE-ing the structures of Sec1/Munc18 proteins. Current Opinion in Structural Biology, 29, 44-51. doi:10.1016/j.sbi.2014.09.003
URI
https://doi.org/10.1016/j.sbi.2014.09.003
 http://apo.ansto.gov.au/dspace/handle/10238/6482
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