Guo Z et al. (2021), Binding Pattern Reconstructions of FGF-FGFR Bud...

ECB-ART-50548

Front Physiol 2021 Jan 01;12:759370. doi: 10.3389/fphys.2021.759370.

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Binding Pattern Reconstructions of FGF-FGFR Budding-Inducing Signaling in Reef-Building Corals.

Guo Z , Liao X , Chen JY , He C , Lu Z .

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Reef-building corals play an important role in marine ecosystems. However, owing to climate change, ocean acidification, and predation by invasive crown-of-thorns starfish, these corals are declining. As marine animals comprise polyps, reproduction by asexual budding is pivotal in scleractinian coral growth. The fibroblast growth factor (FGF) signaling pathway is essential in coral budding morphogenesis. Here, we sequenced the full-length transcriptomes of four common and frequently dominant reef-building corals and screened out the budding-related FGF and FGFR genes. Thereafter, three-dimensional (3D) models of FGF and FGFR proteins as well as FGF-FGFR binding models were reconstructed. Based on our findings, the FGF8-FGFR3 binding models in Pocillopora damicornis, Montipora capricornis, and Acropora muricata are typical receptor tyrosine kinase-signaling pathways that are similar to the Kringelchen (FGFR) in hydra. However, in P. verrucosa, FGF8 is not the FGFR3 ligand, which is found in other hydrozoan animals, and its FGFR3 must be activated by other tyrosine kinase-type ligands. Overall, this study provides background on the potentially budding propagation signaling pathway activated by the applications of biological agents in reef-building coral culture that could aid in the future restoration of coral reefs.

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	FIGURE 1. Evolutionary phylogenetic tree of FGF8s. (A) Bootstrap consensus tree reconstructed with MEGA X using neighbor-joining with default settings. The values beside the branches represent the percentage of time that a node was supported over 1,000 bootstrap replications. (B) Partially conserved domains of FGF genes.
	FIGURE 2. Evolutionary phylogenetic tree of FGFR3s. (A) Bootstrap consensus tree reconstructed with MEGAX using neighbor-joining with default settings. The values beside the branches represent the percentage of time that a node was supported over 1,000 bootstrap replications. (B) Partially conserved domains of FGFR3 genes.
	FIGURE 3. Constructed de novo models of coral FGF8 proteins. (A–D) Are de novo FGF8 models of P. damicornis, P. verrucosa, M. capricomis and A. muricata, respectively. C-terminals are marked in red and N-terminals are marked in blue.
	FIGURE 4. Homology models of coral FGFR3 dimers. Homology models of P. damicorni, P. verrucosa, M. capricomis and A. muricata FGFR3 dimers are shown in panels (A–D). These reconstructions illustrate that the FGFR3s of the four corals are all classic receptor tyrosine kinases with standard molecular architectural features, including extracellular ligand-binding domains (※), transmembrane helixes (arrows), and juxta-membrane regulatory regions (arcs).
	FIGURE 5. Comparisons of homology-constructed coral FGFR3 dimers with receptor tyrosine kinase templates from the RCSB Protein Data Bank. Superposition results of FGFR3 dimer model structures and related template structures in P. damicorni, P. verrucosa, M. capricomis, and A. muricata are shown in panels (A–D). The FGFR3 dimer structure is shown in yellow and purple, and the template structure is shown in green and cyan. The high degree of overlap indicates that coral FGFR3 dimers and receptor tyrosine kinase templates are highly coincident, confirming that the four coral FGFR3s are all tyrosine kinase receptors.
	FIGURE 6. Sequence comparison between FGFR3 in P. damicornis and its template. The same or similar residues are highlighted in blue and dissimilar ones are highlighted in red, with darker blue indicating more similar residues and darker red indicating more dissimilar residues. The sequences corresponding to alpha helixes and beta strands are marked with red and yellow lines, respectively. The FGFR3 dimer structure is basically consistent with the template structure.
	FIGURE 7. FGF8-FGFR3 binding pattern docked by ClusPro in P. damicornis. (A) The interaction between Pd_FGF8 and Pd_FGFR3. (B) The surface binding model of Pd_FGF8 and Pd_FGFR3. Pd_FGFR3 chain A is bright green, Pd_FGFR3 chain B is colored pea green and Pd_FGF8 is colored pink. (C) Details of the interaction between Pd_FGF8 and Pd_FGFR3. The residues in Pd_FGFR3 are green, and in Pd_FGF8 are pink. The red dashes represent hydrogen bond interactions and the blue dashes represent salt bridges.
	FIGURE 8. FGF8-FGFR3 binding pattern docked by ClusPro in P. verrucosa. (A) The interaction between Pv_FGF8 and Pv_FGFR3. (B) Surface binding model of Pv_FGF8 and Pv_FGFR3. Pd_FGFR3 chain A is colored lightpurple, Pd-FGFR3 chain B is colored aquamarine, and Pd_FGF8 is orange. (C) Details of the interaction between Pv_FGF8 and Pv_FGFR3. The residues in Pv_FGFR3 are cyan, and in Pv_FGF8 they are orange. The red dashes represent hydrogen bond interactions and the blue dashes represent salt bridges. Interaction sites between FGFR3 and FGF8 occur only in FGFR3 chain A, which simultaneously falls into the lipid bilayer of the cell membrane, a situation that does not make sense. Pb, phospholipid bilayer of cell membrane.

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