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. 2015 Sep 15;26(18):3245–3262. doi: 10.1091/mbc.E15-06-0366

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© 2015 Merlini et al. This article is distributed by The American Society for Cell Biology under license from the author(s). Two months after publication it is available to the public under an Attribution–Noncommercial–Share Alike 3.0 Unported Creative Commons License (http://creativecommons.org/licenses/by-nc-sa/3.0).

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FIGURE 7: — Syp1 contributes to fast septin recruitment at the bud neck and interacts with Fks1. (A) Kinetics of septin recruitment at the presumptive bud site were calculated by measuring the fluorescence intensity of GFP-Cdc12 over time (frames every 1 min) in cells with the indicated genotypes arrested in G1 by α-factor and released into fresh medium at 30°C at time 0. Wild type, n = 9; syp1Δ, n = 18; SYP1-3A, n = 10; SYP1-3D, n = 15. (B) Mass spectrometric analysis of Flag immunoprecipitates from cell extracts of wild-type cells expressing either untagged Syp1 (mock) or Flag-tagged Syp1 (Syp1-3xFlag) and carrying either wild-type PKC1 or PKC1 deletion (pkc1Δ). Cells were grown to exponential phase in sorbitol-containing medium to keep pkc1Δ cells alive. The table contains only a partial list of Syp1-interacting proteins that were uncovered by mass spectrometry. Unique peptides are peptides with different amino acid sequence. PSM (peptide-spectrum match) represents the total number of peptides identified for each protein. (C) Syp1-3Flag was immunoprecipitated from wild-type and pkc1Δ cells grown in YEPD containing sorbitol. Immunoprecipitates were separated by SDS–PAGE electrophoresis and analyzed by Western blot with anti-Fks1 and anti-Flag antibodies.