Gating of the TrkH ion channel by its associated RCK protein TrkA

Yu Cao, Yaping Pan, Hua Huang, Xiangshu Jin, Elena J. Levin, Brian Kloss and Ming Zhou ()
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Yu Cao: College of Physicians and Surgeons, Columbia University, 630 West 168th Street, New York, New York 10032, USA
Yaping Pan: College of Physicians and Surgeons, Columbia University, 630 West 168th Street, New York, New York 10032, USA
Hua Huang: College of Physicians and Surgeons, Columbia University, 630 West 168th Street, New York, New York 10032, USA
Xiangshu Jin: National Institute of Biological Sciences
Elena J. Levin: College of Physicians and Surgeons, Columbia University, 630 West 168th Street, New York, New York 10032, USA
Brian Kloss: New York Consortium on Membrane Protein Structure, New York Structural Biology Center
Ming Zhou: College of Physicians and Surgeons, Columbia University, 630 West 168th Street, New York, New York 10032, USA

Nature, 2013, vol. 496, issue 7445, 317-322

Abstract: Abstract TrkH belongs to a superfamily of K+ transport proteins required for growth of bacteria in low external K+ concentrations. The crystal structure of TrkH from Vibrio parahaemolyticus showed that TrkH resembles a K+ channel and may have a gating mechanism substantially different from K+ channels. TrkH assembles with TrkA, a cytosolic protein comprising two RCK (regulate the conductance of K+) domains, which are found in certain K+ channels and control their gating. However, fundamental questions on whether TrkH is an ion channel and how it is regulated by TrkA remain unresolved. Here we show single-channel activity of TrkH that is upregulated by ATP via TrkA. We report two structures of the tetrameric TrkA ring, one in complex with TrkH and one in isolation, in which the ring assumes two markedly different conformations. These results suggest a mechanism for how ATP increases TrkH activity by inducing conformational changes in TrkA.

Date: 2013
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DOI: 10.1038/nature12056

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