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. 2021 Aug 6;12:4739. doi: 10.1038/s41467-021-24735-z

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© The Author(s) 2021

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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Fig. 1 — a Strategies of affinity precipitation- and SILAC-based quantitative proteomic analyses of interacting proteins of NAADP (left) and TPCs (right). b Chemical structures of immobilized NAADP. c Numbers of overlapping and non-overlapping putative interacting proteins identified by MS in the indicated four types of affinity-precipitated samples. d Representative heavy-light peak pairs (black) of Lsm12 peptides. Peptide SQAQQPQKEAALS¹⁹⁴ (top) was identified in the samples affinity-purified by immobilized NAADP from TPC1- and TPC2-expressing cells. Peptide LQGEVVAFDYQSK³⁷ was identified in the TPC1 and TPC2 complexes affinity-purified by an anti-FLAG antibody. e Immunoblot of endogenous Lsm12 in samples immunoprecipitated by an anti-FLAG antibody from cells expressing FLAG-tagged TPC1 or TPC2. f Immunoblot of endogenous Lsm12 in samples pulled down by immobilized NAADP from TPC1- and TPC2-expressing cells. AP affinity-precipitation. Exp. transient expression, IB immunoblot.