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. 2017 Aug 7;6(9):1257–1269. doi: 10.1242/bio.025791

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© 2017. Published by The Company of Biologists Ltd

This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/3.0), which permits unrestricted use, distribution and reproduction in any medium provided that the original work is properly attributed.

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Fig. 4. — SNAP-23 phospho mutants and their dynamic membrane association. (A) Sequence alignment showing the SNAP-23WT and other phospho mutants (T102A, S95A/S120A, S95D/S120D) in the linker region. Protein sequences obtained from their respective DNA sequences by using ‘DNA to Protein translation tool’ (http://insilico.ehu.es/translate/index.php). (B) Immunoblots showing the membrane and cytosol association of GFP-SNAP-23 phospho mutants (by SNAP-23-specific antibody). Lanes are cut from the same blots and repositioned (for GFP-SNAP-23 T102A mutant). (C) The band intensities were quantified by spot denso Alpha EaseFC software. The percentage membrane association of SNAP-23 reveals that the mutation of the above residues affects SNAP-23 dynamic association as well as cytosolic accumulation. Each data point is mean±s.e.m. of three independent experiments (*P≤0.05; **P≤0.005; ***P≤0.0005; NS, not significant; Student's t-test, one-tailed distribution).