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. 2022 Jun 23;13:3588. doi: 10.1038/s41467-022-31364-7

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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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Fig. 2 — a A list of ten hnRNPH1-interacting partners in mouse adult WT testes identified by IP-MS is shown. b GO and KEGG term enrichment analyses showing the hnRNPH1-interacting proteins identified from IP-MS data. c The String 10.5 program (http://string-db.org) analyses showing the protein interaction networks among 17 candidate proteins associated with mRNA splicing. d Validation of interactions between hnRNPH1 and three putative hnRNPH1-interacting proteins (PTBP2, SRSF3, and SNRNP70) in mouse testes by in vivo co-immunoprecipitation (Co-IP) assays are shown. IgG was used as a negative control. e Co-immunofluorescence staining of PTBP2 (left panels) and SRSF3 (right panels) with hnRNPH1 in adult mouse testes. P pachytene spermatocytes, RS round spermatids, ES elongated spermatids. DNA was stained with DAPI. Scale bars = 50 µm. f–i Reciprocal Co-IP assays of interaction domains between hnRNPH1 and its binding partners PTBP2 and SRSF3. HEK293T cells were co-transfected with MYC-PTBP2 and the indicated fragments of FLAG-hnRNPH1(f), or co-transfected with FLAG-hnRNPH1 and the indicated fragments of MYC-PTBP2 (g), or co-transfected with MYC-SRSF3 and the indicated fragments of FLAG-hnRNPH1(h), or co-transfected with FLAG-hnRNPH1 and the indicated fragments of MYC-SRSF3 (i), immunoprecipitated with anti-FLAG antibody, and immunoblotted with FLAG and MYC antibodies. Biologically independent experiment (n = 3) were examined (d–i). Source data are provided as a source data file.