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. 2021 Nov 15;11:22237. doi: 10.1038/s41598-021-01481-2

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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 licence, and indicate if changes were made. The images or other third party material in this article are included in the article's Creative Commons licence, unless indicated otherwise in a credit line to the material. If material is not included in the article's Creative Commons licence 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 licence, visit http://creativecommons.org/licenses/by/4.0/.

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Molecular design and cellular localization of FP-inserted γB2. (a) Schematics of full-length protocadherin-γB2 (γB2). γB2 is represented as serially repeated extracellular domains (EC domains), a transmembrane region (TM), and a cytoplasmic region (Cyto). The insertion positions (amino acid position 29th and 472nd residues in the matured form) of fluorescent protein (FP) are indicated by yellow arrowheads. (b) The localization of Venus-inserted γB2 constructs in HEK293T cells. HEK293T cells expressing the indicated constructs were observed using a confocal microscope. Fluorescence images (upper) and merged fluorescence and differential interference contrast (DIC) images (lower) are shown. Scale bar, 20 μm. (c) Schematics of FP-inserted γB2ΔICDs. In γB2ΔICD-EC1-mTQ2 and γB2ΔICD-EC5-Venus, mTurquoise2 (mTQ2) and Venus are inserted in γB2ΔICD at the positions as indicated in (a). ΔICD denotes deletion of an intracellular domain (ICD), which leads to efficient localization of γB2 at the plasma membrane. (d) The localization of FP-inserted γB2ΔICDs in HEK293T cells. HEK293T cells expressing the indicated constructs were observed using a confocal microscope. Scale bar, 20 μm.