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-Structure paper
| タイトル | Structure reveals a regulation mechanism of plant outward-rectifying K channel GORK by structural rearrangements in the CNBD-Ankyrin bridge. |
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| ジャーナル・号・ページ | Proc Natl Acad Sci U S A, Vol. 122, Issue 30, Page e2500070122, Year 2025 |
| 掲載日 | 2025年7月29日 |
著者 | Taro Yamanashi / Yuki Muraoka / Tadaomi Furuta / Tsukasa Kume / Natsuko Sekido / Shunya Saito / Shota Terashima / Takeshi Yokoyama / Yoshikazu Tanaka / Atsushi Miyamoto / Kanane Sato / Tomoyuki Ito / Hikaru Nakazawa / Mitsuo Umetsu / Ellen Tanudjaja / Masaru Tsujii / Ingo Dreyer / Julian I Schroeder / Yasuhiro Ishimaru / Nobuyuki Uozumi / ![]() |
| PubMed 要旨 | Guard cells, which regulate stomatal apertures in plants, possess a sophisticated mechanism for regulating turgor pressure. The outward-rectifying "K" channel GORK, expressed in guard cells of the ...Guard cells, which regulate stomatal apertures in plants, possess a sophisticated mechanism for regulating turgor pressure. The outward-rectifying "K" channel GORK, expressed in guard cells of the plant , is a central component that promotes stomatal closure by releasing K to the extracellular space, thereby lowering turgor pressure. To date, the structural basis underlying the regulation of the K transport activity of GORK is unclear. Using cryo-EM, we determined the structures of the GORK outward-rectifying K channel with a resolution of 3.16 to 3.27 Å in five distinct conformations that differ significantly in their C-terminal cyclic nucleotide binding domain (CNBD) and ankyrin repeat (ANK) domain. The C-linker connects the transmembrane domains to the C-terminal domains, i.e., CNBD, CNBD-Ankyrin bridge, and ANK. The structural changes and interactions in the C-linker determine whether the closed state of GORK is closer to the preopen state or in a more removed state from the open state of the channel. In particular, interconversion in the short sequence within the CNBD-Ankyrin bridge plays a decisive role in this determination. This region forms an α-helix in the preopened state, while it adopts a nonhelical structure in further distant closed states. The dynamics of the cytosolic region strongly suggest that the K channel activity of GORK is regulated by cytosolic signaling factors during stomatal closure. |
リンク | Proc Natl Acad Sci U S A / PubMed:40699930 / PubMed Central |
| 手法 | EM (単粒子) |
| 解像度 | 2.39 - 3.2 Å |
| 構造データ | EMDB-62913, PDB-9l9u: EMDB-62915, PDB-9la0: EMDB-62916, PDB-9la1: EMDB-62917, PDB-9la2: EMDB-62918, PDB-9la3: EMDB-62921, PDB-9la7: |
| 由来 |
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キーワード | PLANT PROTEIN / Outward potassium channel in stomata |
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