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. 2022 May 23;20:81. doi: 10.1186/s12958-022-00953-y

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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/. The Creative Commons Public Domain Dedication waiver (http://creativecommons.org/publicdomain/zero/1.0/) applies to the data made available in this article, unless otherwise stated in a credit line to the data.

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Fig. 2 — Kisspeptin/KISS1R signalings. When kisspeptin binds to the seven-transmembrane domain receptor, KISS1R, the intracellular portion of KISS1R leads to the phosphorylation of Gq/11. The α-subunit of Gq/11 then activates PLC, which subsequently cleaves PIP2 into IP3 and DAG. IP3 promotes intracellular Ca2+ release from the endoplasmic reticulum, while DAG promotes the phosphorylation of PKC which further induces the phosphorylation of ERK1/2 and p38. DAG, diacylglycerol; ERK1/2, extracellular signal-regulated kinase; IP3, inositol 1,4,5-triphosphate; PI3K, phosphatidylinositol-3-kinase; PIP2, phosphatidylinositol 4,5-bisphosphate; PKC, protein kinase C; PLC, phospholipase C. Modified from [17]