Abstract
Evolution often diversifies a peptide hormone family into multiple subfamilies, which exert distinct activities by exclusive interaction with specific receptors. Here we show that systematic swapping of pre-existing variation in a subfamily of plant CLE peptide hormones leads to a synthetic bifunctional peptide that exerts activities beyond the original subfamily by interacting with multiple receptors. This approach provides new insights into the complexity and specificity of peptide signalling.
| Original language | English |
|---|---|
| Article number | 14318 |
| Journal | Nature Communications |
| Volume | 8 |
| DOIs | |
| State | Published - Feb 6 2017 |
| Externally published | Yes |
Funding
This research was supported by MEXT/JSPS KAKENHI (grant numbers JP26113507, JP26291057 and JP16H01237 to K.U.T; JP25114511, JP26113707 and JP16H01462 to N.U.; JP25221105 and JP15H05957 to Y.M; JP26113520, JP16H01234 and JP25840111 to H.S.) and Howard Hughes Medical Institute (HHMI) and Gordon and Betty Moore Foundation (GBMF) (grant number GBMF3035 to K.U.T). K.U.T. is an HHMI-GBMF Investigator. Y.H. and K.W. are JSPS Postdoctoral Fellows. Y.H. was an HFSP Postdoctoral Fellow