Structure and Function of Voltage-Dependent Ion Channel Regulatory β Subunits†

Biochemistry ◽  
2002 ◽  
Vol 41 (9) ◽  
pp. 2886-2894 ◽  
Author(s):  
M. R. Hanlon ◽  
B. A. Wallace
Author(s):  
G. JUNG ◽  
R.-P. HUMMEL ◽  
K.-P. VOGES ◽  
C. TONIOLO ◽  
G. BOHEIM

2016 ◽  
Vol 148 (2) ◽  
pp. 97-118 ◽  
Author(s):  
Thomas E. DeCoursey ◽  
Deri Morgan ◽  
Boris Musset ◽  
Vladimir V. Cherny

The voltage-gated proton channel (HV1) is a widely distributed, proton-specific ion channel with unique properties. Since 2006, when genes for HV1 were identified, a vast array of mutations have been generated and characterized. Accessing this potentially useful resource is hindered, however, by the sheer number of mutations and interspecies differences in amino acid numbering. This review organizes all existing information in a logical manner to allow swift identification of studies that have characterized any particular mutation. Although much can be gained from this meta-analysis, important questions about the inner workings of HV1 await future revelation.


2011 ◽  
Vol 39 (3) ◽  
pp. 707-718 ◽  
Author(s):  
René A.W. Frank

Ionotropic receptors, including the NMDAR (N-methyl-D-aspartate receptor) mediate fast neurotransmission, neurodevelopment, neuronal excitability and learning. In the present article, the structure and function of the NMDAR is reviewed with the aim to condense our current understanding and highlight frontiers where important questions regarding the biology of this receptor remain unanswered. In the second part of the present review, new biochemical and genetic approaches for the investigation of ion channel receptor complexes will be discussed.


2011 ◽  
Vol 301 (4) ◽  
pp. F684-F696 ◽  
Author(s):  
Ossama B. Kashlan ◽  
Thomas R. Kleyman

Our understanding of epithelial Na+ channel (ENaC) structure and function has been profoundly impacted by the resolved structure of the homologous acid-sensing ion channel 1 (ASIC1). The structure of the extracellular and pore regions provide insight into channel assembly, processing, and the ability of these channels to sense the external environment. The absence of intracellular structures precludes insight into important interactions with intracellular factors that regulate trafficking and function. The primary sequences of ASIC1 and ENaC subunits are well conserved within the regions that are within or in close proximity to the plasma membrane, but poorly conserved in peripheral domains that may functionally differentiate family members. This review examines functional data, including ion selectivity, gating, and amiloride block, in light of the resolved ASIC1 structure.


2018 ◽  
Vol 43 (6) ◽  
pp. 436-451 ◽  
Author(s):  
Viktoria Klippenstein ◽  
Laetitia Mony ◽  
Pierre Paoletti

2021 ◽  
Author(s):  
Philipp A.M. Schmidpeter ◽  
Crina M. Nimigean

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