DRP1A is enriched in DRMs and co-localizes with sterols at the cell plate.(a–d) Western blot analysis of DRM fractions from 3-week-old Arabidopsis callus cultures of wild-type L er and the cpi1 - 1 mutant (in the L er background). Equal amounts of membrane protein were loaded from the control fraction mock-extracted at a Triton X-100 detergent/protein (w/w) ratio of 0 (non-DRM) and the DRM fraction extracted at a Triton X-100 detergent/protein (w/w) ratio of 8 (DRM). Similar results were obtained in three independent experiments.(a) Western blot from DRM extractions probed with anti-DRP1A (isoform-specific), anti-CLC (generic), anti-ARF1 (generic) and anti-SMT1 (isoform-specific) antibodies.(b) Replicate Coomassie Blue gel as a loading control for the blot in (a).(c) Western blot from DRM extraction probed with anti-CHC (generic) and anti-SMT1 (isoform-specific) antibodies.(d) Replicate Coomassie Blue gel as a loading control for the blot in (c).The results in (a) and (c) indicate enrichment of DRP1A, CLC2, CHC and ARF1 in DRMs compared to depleted SMT1.(e–m) Co-localization analyses at the cell plate in late cytokinetic cells: (e,h,k) filipin-sterol fluorescence (fil, red); (f) DRP1A–GFP, (i) DRP2B–GFP and (l) CLC2–GFP fluorescence (green). (g,j,m) Merged images of (e) and (f), (h) and (i), and (k) and (l), respectively. Scale bars = 5 μm.