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TitleStructure reveals a regulation mechanism of plant outward-rectifying K channel GORK by structural rearrangements in the CNBD-Ankyrin bridge.
Journal, issue, pagesProc Natl Acad Sci U S A, Vol. 122, Issue 30, Page e2500070122, Year 2025
Publish dateJul 29, 2025
AuthorsTaro 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 AbstractGuard 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.
External linksProc Natl Acad Sci U S A / PubMed:40699930 / PubMed Central
MethodsEM (single particle)
Resolution2.39 - 3.2 Å
Structure data

62913

9l9u

EMDB-62913, PDB-9l9u:
Arabidopsis GORK WT1
Method: EM (single particle) / Resolution: 3.12 Å

62915

9la0

EMDB-62915, PDB-9la0:
Arabidopsis GORK WT5
Method: EM (single particle) / Resolution: 3.1 Å

62916

9la1

EMDB-62916, PDB-9la1:
Arabidopsis GORK WT4
Method: EM (single particle) / Resolution: 3.15 Å

62917

9la2

EMDB-62917, PDB-9la2:
Arabidopsis GORK WT2
Method: EM (single particle) / Resolution: 3.2 Å

62918

9la3

EMDB-62918, PDB-9la3:
Arabidopsis GORK WT3
Method: EM (single particle) / Resolution: 3.19 Å

62921

9la7

EMDB-62921, PDB-9la7:
Arabidopsis GORK consensus structure
Method: EM (single particle) / Resolution: 2.39 Å

Source
  • arabidopsis thaliana (thale cress)
KeywordsPLANT PROTEIN / Outward potassium channel in stomata

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