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-Structure paper
| タイトル | Structural and mechanistic insights into symmetry conversion in plant GORK K+ channel regulation. |
|---|---|
| ジャーナル・号・ページ | Protein Cell, Vol. 16, Issue 12, Page 1035-1047, Year 2025 |
| 掲載日 | 2025年12月1日 |
著者 | Qi-Yu Li / Li Qin / Ling-Hui Tang / Chun-Rui Zhang / Shouguang Huang / Ke Wang / Gao-Hua Zhang / Ning-Jie Hao / Qian Xiao / Tongxin Niu / Min Su / Rainer Hedrich / Yu-Hang Chen / ![]() |
| PubMed 要旨 | GORK is a shaker-like potassium channel in plants that contains ankyrin (ANK) repeats. In guard cells, activation of GORK causes K+ efflux, reducing turgor pressure and closing stomata. However, how ...GORK is a shaker-like potassium channel in plants that contains ankyrin (ANK) repeats. In guard cells, activation of GORK causes K+ efflux, reducing turgor pressure and closing stomata. However, how GORK is regulated remains largely elusive. Here, we solved the cryo-EM structure of Arabidopsis GORK, revealing an unusual symmetry reduction (from C4 to C2) feature within its tetrameric assembly. This symmetry reduction in GORK channel is driven by ANK dimerization, which disrupts the coupling between transmembrane helices and cytoplasmic domains, thus maintaining GORK in an autoinhibited state. Electrophysiological and structural analyses further confirmed that ANK dimerization inhibits GORK, and its removal restores C4 symmetry, converting GORK to an activatable state. This dynamic switching between C2 and C4 symmetry, mediated by ANK dimerization, presents a GORK target site that guard cells regulate to switch the plant K+ channel between inhibited and activatable states, thus controlling stomatal movement in response to environmental stimuli. |
リンク | Protein Cell / PubMed:40996076 / PubMed Central |
| 手法 | EM (単粒子) |
| 解像度 | 3.2 - 4.3 Å |
| 構造データ | EMDB-37500, PDB-8wfz: EMDB-62337, PDB-9khe: EMDB-62338, PDB-9khf: EMDB-62339, PDB-9khg: |
| 化合物 | ![]() ChemComp-K: |
| 由来 |
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キーワード | TRANSPORT PROTEIN / Complex / Protein / PLANT PROTEIN / PROTON TRANSPORT |
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