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. 2022 May 24;64(12):1319–1327. doi: 10.1007/s12033-022-00504-1

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© The Author(s) 2022

Open AccessThis 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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Fig. 1 — Protein domains of human PAR6, aPKC, and PAR3. PAR6 and aPKC interact via their PB1 domains. aPKC harbors a kinase domain that can phosphorylate PAR3 followed by PAR3 release from the complex. PAR3 binds to PAR6–aPKC via a PDZ/aPKC-binding domain. The neural isoform analyzed herein showed alternative splicing leading to an extra mini-exon at amino acid (aa) 270, an omission of 3 amino acids at aa 739–743, and a skipped exon encoding aa 1024–1062 (positions compared to the canonical PAR3 sequence, accession no. NP_062565.2)