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. 2022 Jul 12;3:931331. doi: 10.3389/fragi.2022.931331

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Copyright © 2022 Prud’homme, Kurt and Wang.

This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner(s) are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.

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The Klotho/FGFR/FGF23 signaling complex. Klotho interacts with a FGFR (frequently FGFR1c) through an extension of its KL2 domain. FGF23 fits into a groove formed by components of KL1, KL2 and the FGFR. The membrane-bound and soluble Klotho forms (KL1/KL2 domains) can both bind to FGFR1c and function as coreceptors (Chen G, et al., 2018). These molecular interactions create a high affinity binding site for FGF23. The activated FGFR signals through multiple pathways as illustrated, and outlined in the text. Abbreviations: ERK, extracellular signal-regulated kinase; FGF23, fibroblast growth factor 23; FGFR1-c, FGF receptor 1c; MAPK, mitogen-activated protein kinase; PI3K, phosphoinositide 3-kinase; PKC, protein kinase C; PLCγ, phospholipase Cγ.