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. 2022 Dec 15;30(1):52–61. doi: 10.1038/s41594-022-00899-0

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© The Author(s) 2022

Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/.

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Extended Data Fig. 1 — a, Identification of all five subunits in isolated endogenous LRRC8 complexes from HEK293T cells by shotgun LC-MS/MS. b, c, VRAC currents recorded in the whole-cell configuration in response to a change of the extracellular environment to hypotonic conditions. Values show average of three biological replicates recorded at 100 mV in, b, HEK293T and, c, LRRC8^B,D,E,-/- cells. Errors are s.e.m. The changes in extracellular osmolarity are indicated (top). Insets show traces of a representative cell recorded at different voltages at the plateau of activation. d, LRRC8A/C precursor and product ion masses used for absolute quantification. Asterisk denotes heavy labeled residues. e, Determination of absolute peptide levels in isolated LRRC8 complexes using LC-MS/MS. Peptide amounts on column (fmol) were calculated using the ratio of endogenous and SIL (stable-isotope labeled) peptides: IEAPALAFLR (1) and YIVIDGLR (2) from LRRC8A and NSLSVLSPK (3) and YLDLSYNDIR (4) from LRRC8C. Graphs show individual biological replicates with bars representing the average of the two peptides belonging to the same subunit.

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