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. 2020 Oct 2;6(40):eabb7854. doi: 10.1126/sciadv.abb7854

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Copyright © 2020 The Authors, some rights reserved; exclusive licensee American Association for the Advancement of Science. No claim to original U.S. Government Works. Distributed under a Creative Commons Attribution NonCommercial License 4.0 (CC BY-NC).

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Fig. 5 — Immunoblot (IB) analysis (A) and quantitation (B) showing changes in actin polymerization (F-actin in the insoluble fraction) following washout after treatment with the actin depolymerizing agent latrunculin A (LatA). Data are means ± SEM (n = 4). (C) IB analysis using anti-Me3^K68 antibody showing that ActK68me3 occurs on endogenous actin from the insoluble F-actin fraction of SETD2-proficient 786-0 cells; tubulin (which is also methylated by SETD2) is not found in this fraction. Data are representative of experiments repeated at least three times with similar results. Absence of H3K36me3 in the insoluble fraction is used as a control to confirm loss of SETD2 in (A) and (C). (D) IP of actin using anti-Me3^K68 antibody from soluble (G-actin) and insoluble (F-actin) fractions of SETD2-proficient cells treated with LatA for indicated times. Light and dark exposures are shown for contrast in amount of methylated actin between fractions. Data are representative of three experiments performed using anti-Me3^K68 and anti-Me3^Pan antibodies with similar results. In an additional experiment performed shortly after cells were brought up from cryopreservation, we saw a less marked loss of methylated insoluble actin with LatA, but saw no increase in methylated soluble actin, consistent with data shown here.