Contact
Positions
Assistant Professor
- Organization:
- West Virginia University School of Medicine
- Department:
- Biochemistry and Molecular Medicine
- Classification:
- Faculty
Education
- BS, Capital Normal University, 2010
- PhD, Texas A&M University, 2016
Publications
Selected papers:
Liu, S., Payne, A.M., Wang, J. et al. Architecture and activation of single-pass transmembrane receptor guanylyl cyclase. Nat Struct Mol Biol 32, 469–478 (2025).
Liu, S.*, Paknejad, N.*, Zhu, L. et al. Differential activation mechanisms of lipid GPCRs by lysophosphatidic acid and sphingosine 1-phosphate. Nat Commun 13, 731 (2022).
Liu, S., Gonen, T. MicroED structure of the NaK ion channel reveals a Na+ partition process into the selectivity filter. Commun Biol 1, 38 (2018).
Liu S., Focke P.J., Matulef K., Bian X., Moënne-Loccoz P., Valiyaveetil F.I., Lockless S.W. Ion-binding properties of a K+ channel selectivity filter in different conformations. Proc Natl Acad Sci U S A. 2015 Dec 8;112(49):15096-100.
Huang H.*, Levin E.J.*, Liu S., Bai Y., Lockless S.W., Zhou M. (2014) Structure of a Membrane-Embedded Prenyltransferase Homologous to UBIAD1. PLoS Biol 12(7): e1001911.
Liu, S., Lockless, S. Equilibrium selectivity alone does not create K+-selective ion conduction in K+ channels. Nat Commun 4, 2746 (2013).
Liu X., Liu S., Feng Y., Liu J.Z., Chen Y., Pham K., Deng H., Hirschi K.D., Wang X., Cheng N.. Structural insights into the N-terminal GIY-YIG endonuclease activity of Arabidopsis glutaredoxin AtGRXS16 in chloroplasts. Proc Natl Acad Sci U S A. 2013 Jun 4;110(23):9565-70.
Liu S.*, Bian X.*, Lockless S.W.. Preferential binding of K+ ions in the selectivity filter at equilibrium explains high selectivity of K+ channels. J Gen Physiol. 2012 Dec;140(6):671-9.
*co-first author
Research Interests
-
Membrane protein structures and biophysics
-
Drug development
Receptor Guanyly Cyclase
Receptor guanylyl cyclases (rGCs) are a family of membrane-bound enzymes that directly synthesize the second messenger cGMP from GTP in response to diverse signaling cues. By elevating intracellular cGMP levels, rGCs regulate a wide range of physiological processes, including blood pressure control, bone development, intestinal water and solute homeostasis, and vision.
Recently, Dr. Liu in his postdoctoral training determined the first full-length structures of GC-A in both inactive and active states using single-particle cryo-EM. Building on these findings, the Liu lab will continue to investigate the molecular mechanisms underlying rGC activation and to develop therapeutic strategies aimed at modulating their activity.
G protein-coupled Receptor
G protein–coupled receptors (GPCRs) constitute the largest protein family in the human genome and detect a wide range of extracellular signals, including hormones, neurotransmitters, sensory stimuli, and chemokines. Upon activation, GPCRs transduce these signals into the cell to regulate numerous physiological processes, such as metabolism, immune responses, vision, and neural activity, making them one of the most important and extensively targeted classes in therapeutic drug development.
Our lab employs biochemical, biophysical, and structural biology approaches to elucidate the activation mechanisms of GPCRs and to develop drugs targeting these receptors.