TrkA undergoes a tetramer-to-dimer conversion to open TrkH which enables changes in membrane potential

Zhang, Hanzhi; Pan, Yaping; Hu, Liya; Hudson, M. Ashley; Hofstetter, Katrina S.; Xu, Zhichun; Rong, Mingqiang; Wang, Zhao; Prasad, B. V.  Venkataram; Lockless, Steve W.; Chiu, Wah; Zhou, Ming

doi:10.1038/s41467-019-14240-9

Title: TrkA undergoes a tetramer-to-dimer conversion to open TrkH which enables changes in membrane potential

Journal Article · 28 January 2020 · Nature Communications

DOI: https://doi.org/10.1038/s41467-019-14240-9 · OSTI ID:1598012

Zhang, Hanzhi ^[1]; Pan, Yaping ^[1];

^[1]; Hudson, M. Ashley ^[2]; Hofstetter, Katrina S. ^[2]; Xu, Zhichun ^[1]; Rong, Mingqiang ^[1];

^[1];

^[1]; Lockless, Steve W. ^[2]; Chiu, Wah ^[3]; Zhou, Ming ^[1]

Baylor College of Medicine, Houston, TX (United States)
Texas A & M Univ., College Station, TX (United States)
Stanford Univ., CA (United States)

TrkH is a bacterial ion channel implicated in K⁺ uptake and pH regulation. TrkH assembles with its regulatory protein, TrkA, which closes the channel when bound to ADP and opens it when bound to ATP. However, it is unknown how nucleotides control the gating of TrkH through TrkA. Here we report the structures of the TrkH-TrkA complex in the presence of ADP or ATP. TrkA forms a tetrameric ring when bound to ADP and constrains TrkH to a closed conformation. The TrkA ring splits into two TrkA dimers in the presence of ATP and releases the constraints on TrkH, resulting in an open channel conformation. Functional studies show that both the tetramer-to-dimer conversion of TrkA and the loss of constraints on TrkH are required for channel gating. In addition, deletion of TrkA in Escherichia coli depolarizes the cell, suggesting that the TrkH-TrkA complex couples changes in intracellular nucleotides to membrane potential.

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Research Organization:: Argonne National Laboratory (ANL), Argonne, IL (United States). Advanced Photon Source (APS)

Sponsoring Organization:: National Institutes of Health (NIH); Cancer Prevention and Research Institute of Texas (CPRIT); Robert Welch Foundation

Grant/Contract Number:: HL086392; DK122784; P41GM103832; GM132436; R1223; Q-1279; Q-1967; A-1742; AC02-06CH11357

OSTI ID:: 1598012

Journal Information:: Nature Communications, Vol. 11, Issue 1; ISSN 2041-1723

Publisher:: Nature Publishing GroupCopyright Statement

Country of Publication:: United States

Language:: ENGLISH

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Cited by: 15 works

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Understanding the Molecular Dynamics of Type-2 Diabetes Drug Target DPP-4 and its Interaction with Sitagliptin and Inhibitor Diprotin-A Chakraborty, Chiranjib; Hsu, Minna J.; Agoramoorthy, Govindasamy Cell Biochemistry and Biophysics, Vol. 70, Issue 2 https://doi.org/10.1007/s12013-014-9998-0	journal	May 2014
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Crystal structures of multidrug efflux pump MexB bound with high-molecular-mass compounds Sakurai, Keisuke; Yamasaki, Seiji; Nakao, Kaori Scientific Reports, Vol. 9, Issue 1 https://doi.org/10.1038/s41598-019-40232-2	journal	March 2019
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High throughput in silico identification and characterization of Plasmodium falciparum PRL phosphatase inhibitors Pandey, Rajan; Kumar, Rakesh; Gupta, Priya Journal of Biomolecular Structure and Dynamics, Vol. 36, Issue 13 https://doi.org/10.1080/07391102.2017.1392365	journal	November 2017
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Comparative structural analysis of the caspase family with other clan CD cysteine peptidases McLuskey, Karen; Mottram, Jeremy C. Biochemical Journal, Vol. 466, Issue 2 https://doi.org/10.1042/BJ20141324	journal	February 2015
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The intrinsic structure of poly(A) RNA determines the specificity of Pan2 and Caf1 deadenylases Tang, Terence T. L.; Stowell, James A. W.; Hill, Chris H. Nature Structural & Molecular Biology, Vol. 26, Issue 6 https://doi.org/10.1038/s41594-019-0227-9	journal	May 2019

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