Electrostatic anchoring precedes stable membrane attachment of SNAP25/SNAP23 to the plasma membrane
- University of Bonn, Germany
- Heidelberg University Biochemistry Center, Germany
Abstract
The SNAREs SNAP25 and SNAP23 are proteins that are cytosolic after translation, but then become stably attached to the cell membrane through palmitoylation of cysteine residues. For palmitoylation to occur, membrane association is a prerequisite, but it is unclear which motif may increase the affinities of the proteins to the target membrane. In experiments with rat neuroendocrine cells, we find that a few polybasic amino acids in the cysteine rich region are essential for plasma membrane targeting. Reconstitution of membrane-protein binding in a liposome assay shows that the mechanism involves protein electrostatics between polybasic amino acid residues and anionic lipids like phosphoinositides that play a primary role in these interactions. Hence, we identify an electrostatic anchoring mechanism underlying initial contact establishment of SNARE proteins which then subsequently become palmitoylated at the plasma membrane.
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Funding
Deutsche Forschungsgemeinschaft (TRR83)
- Thomas Söllner
Deutsche Forschungsgemeinschaft (TRR83)
- Thorsten Lang
The funders had no role in study design, data collection and interpretation, or the decision to submit the work for publication.
Copyright
© 2017, Weber et al.
This article is distributed under the terms of the Creative Commons Attribution License permitting unrestricted use and redistribution provided that the original author and source are credited.
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Electrostatic anchoring precedes stable membrane attachment of SNAP25/SNAP23 to the plasma membrane
eLife 6:e19394.
https://doi.org/10.7554/eLife.19394
