Journal article
The nature of the Syntaxin4 C-terminus affects Munc18c-supported SNARE assembly
A Rehman, SH Hu, Z Tnimov, AE Whitten, GJ King, RJ Jarrott, SJ Norwood, K Alexandrov, BM Collins, MP Christie, JL Martin
Plos One | PUBLIC LIBRARY SCIENCE | Published : 2017
Open access
Abstract
Vesicular transport of cellular cargo requires targeted membrane fusion and formation of a SNARE protein complex that draws the two apposing fusing membranes together. Insulin-regulated delivery and fusion of glucose transporter-4 storage vesicles at the cell surface is dependent on two key proteins: the SNARE integral membrane protein Syntaxin4 (Sx4) and the soluble regulatory protein Munc18c. Many reported in vitro studies of Munc18c:Sx4 interactions and of SNARE complex formation have used soluble Sx4 constructs lacking the native transmembrane domain. As a consequence, the importance of the Sx4 C-terminal anchor remains poorly understood. Here we show that soluble C-terminally truncated ..
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Awarded by China Scholarship Council
Funding Acknowledgements
This work was supported by the Australian National Health and Medical Research Council (NHMRC) program grant 535921 and project grant 1066069. At the time of this work, AEW was supported by an NHMRC Peter Doherty Fellowship (569864); KA was an ARC Future Fellow (FT0991611); BMC was an ARC Future Fellow (FT100100027) and is now an NHMRC Career Development Fellow (APP1061574); and JLM was an ARC Australian Laureate Fellow (FL0992138) and honorary NHMRC Fellow (APP455829). The funders had no role in study design, data collection and analysis, decision to publish, or preparation of the manuscript.