Endogenous ion channel complexes: the NMDA receptor

2011 ◽  
Vol 39 (3) ◽  
pp. 707-718 ◽  
Author(s):  
René A.W. Frank
Keyword(s):  
Nmda Receptor ◽  
Ion Channel ◽  
Present Article ◽  
Neuronal Excitability ◽  
Structure And Function ◽  
Current Understanding ◽  
Ionotropic Receptors ◽  
Receptor Complexes ◽  
Aspartate Receptor ◽  
And Function

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.

scholarly journals Insights into the structure and function of HV1 from a meta-analysis of mutation studies

2016 ◽  
Vol 148 (2) ◽  
pp. 97-118 ◽  
Author(s):  
Thomas E. DeCoursey ◽  
Deri Morgan ◽  
Boris Musset ◽  
Vladimir V. Cherny
Keyword(s):  
Amino Acid ◽  
Ion Channel ◽  
Meta Analysis ◽  
Structure And Function ◽  
Proton Channel ◽  
Vast Array ◽  
Voltage Gated ◽  
Interspecies Differences ◽  
And Function ◽  
Sheer Number

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.

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
Keyword(s):  
Ion Channel ◽  
Structure And Function ◽  
Voltage Dependent ◽  
And Function

Structure and Function of the Plant Alternative Oxidase: Its Putative Role in the Oxygen Defence Mechanism

1997 ◽  
Vol 17 (3) ◽  
pp. 319-333 ◽  
Author(s):  
Anneke M. Wagner ◽  
Anthony L. Moore
Keyword(s):  
Oxidative Stress ◽  
Alternative Oxidase ◽  
Structure And Function ◽  
Current Understanding ◽  
Defence Mechanism ◽  
Putative Role ◽  
And Function

Current understanding of the structure and function of the plant alternative oxidase is reviewed. In particular, the role of the oxidase in the protection of tissues against oxidative stress is developed.

scholarly journals ENaC structure and function in the wake of a resolved structure of a family member

2011 ◽  
Vol 301 (4) ◽  
pp. F684-F696 ◽  
Author(s):  
Ossama B. Kashlan ◽  
Thomas R. Kleyman
Keyword(s):  
Plasma Membrane ◽  
Ion Channel ◽  
Functional Data ◽  
Ion Selectivity ◽  
External Environment ◽  
Structure And Function ◽  
Close Proximity ◽  
Channel Assembly ◽  
And Function ◽  
Insight Into

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.

scholarly journals The Structure and Function of Ionotropic Receptors in Drosophila

2021 ◽  
Vol 13 ◽  
Author(s):  
Lina Ni
Keyword(s):  
Glutamate Receptors ◽  
Structure And Function ◽  
Ionotropic Glutamate Receptors ◽  
Animal Kingdom ◽  
Ionotropic Receptors ◽  
Ir Studies ◽  
Major Branch ◽  
Future Direction ◽  
And Function ◽  
Peripheral Sensory

Ionotropic receptors (IRs) are a highly divergent subfamily of ionotropic glutamate receptors (iGluR) and are conserved across Protostomia, a major branch of the animal kingdom that encompasses both Ecdysozoa and Lophothrochozoa. They are broadly expressed in peripheral sensory systems, concentrated in sensory dendrites, and function in chemosensation, thermosensation, and hygrosensation. As iGluRs, four IR subunits form a functional ion channel to detect environmental stimuli. Most IR receptors comprise individual stimulus-specific tuning receptors and one or two broadly expressed coreceptors. This review summarizes the discoveries of the structure of IR complexes and the expression and function of each IR, as well as discusses the future direction for IR studies.

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