Potassium Flux through Gramicidin Ion Channels Is Augmented in Vesicles Comprising Plasmenylcholine: Correlations between Gramicidin Conformation and Function in Chemically Distinct Host Bilayer Matrixes

Biochemistry ◽  
1995 ◽  
Vol 34 (22) ◽  
pp. 7356-7364 ◽  
Author(s):  
Xi Chen ◽  
Richard W. Gross
Keyword(s):  
Ion Channels ◽  
Potassium Flux ◽  
And Function

Kinematic Design of Functional Nanoscale Mechanisms From Molecular Primitives

2021 ◽  
Author(s):  
Meysam T. Chorsi ◽  
Pouya Tavousi ◽  
Caitlyn Mundrane ◽  
Vitaliy Gorbatyuk ◽  
Kazem Kazerounian ◽  
...  
Keyword(s):  
Ion Channels ◽  
Range Of Motion ◽  
Systematic Approach ◽  
Design Space ◽  
Vital Role ◽  
Degree Of Freedom ◽  
Living Systems ◽  
Kinematic Design ◽  
Systematic Exploration ◽  
And Function

Abstract Natural nanomechanisms such as capillaries, neurotransmitters, and ion channels play a vital role in the living systems. But the design principles developed by nature through evolution are not well understood and, hence, not applicable to engineered nanomachines. Thus, the design of nanoscale mechanisms with prescribed functions remains a challenge. Here, we present a systematic approach based on established kinematics techniques to designing, analyzing, and controlling manufacturable nanomachines with prescribed mobility and function built from a finite but extendable number of available "molecular primitives." Our framework allows the systematic exploration of the design space of irreducibly simple nanomachines, built with prescribed motion specification by combining available nanocomponents into systems having constrained, and consequently controllable motions. We show that the proposed framework has allowed us to discover and verify a molecule in the form of a seven link, seven revolute (7R) close loop spatial linkage with mobility (degree of freedom) of one. Furthermore, our experiments exhibit the type and range of motion predicted by our simulations. Enhancing such a structure into functional nanomechanisms by exploiting and controlling their motions individually or as part of an ensemble could galvanize development of the multitude of engineering, scientific, medical, and consumer applications that can benefit from engineered nanomachines.

scholarly journals Cellular distribution and function of ion channels involved in transport processes in rat tracheal epithelium

2017 ◽  
Vol 5 (12) ◽  
pp. e13290 ◽  
Author(s):  
Anne Hahn ◽  
Johannes Faulhaber ◽  
Lalita Srisawang ◽  
Andreas Stortz ◽  
Johanna J Salomon ◽  
...  
Keyword(s):  
Ion Channels ◽  
Transport Processes ◽  
Tracheal Epithelium ◽  
Cellular Distribution ◽  
And Function

scholarly journals Site-specific deacylation by ABHD17a controls BK channel splice variant activity

2020 ◽  
Vol 295 (49) ◽  
pp. 16487-16496 ◽  
Author(s):  
Heather McClafferty ◽  
Hamish Runciman ◽  
Michael J. Shipston
Keyword(s):  
Ion Channels ◽  
Ion Channel ◽  
Membrane Trafficking ◽  
Transmembrane Protein ◽  
Surface Expression ◽  
Bk Channels ◽  
Bk Channel ◽  
Site Specific ◽  
And Function ◽  
A Site

S-Acylation, the reversible post-translational lipid modification of proteins, is an important mechanism to control the properties and function of ion channels and other polytopic transmembrane proteins. However, although increasing evidence reveals the role of diverse acyl protein transferases (zDHHC) in controlling ion channel S-acylation, the acyl protein thioesterases that control ion channel deacylation are very poorly defined. Here we show that ABHD17a (α/β-hydrolase domain-containing protein 17a) deacylates the stress-regulated exon domain of large conductance voltage- and calcium-activated potassium (BK) channels inhibiting channel activity independently of effects on channel surface expression. Importantly, ABHD17a deacylates BK channels in a site-specific manner because it has no effect on the S-acylated S0–S1 domain conserved in all BK channels that controls membrane trafficking and is deacylated by the acyl protein thioesterase Lypla1. Thus, distinct S-acylated domains in the same polytopic transmembrane protein can be regulated by different acyl protein thioesterases revealing mechanisms for generating both specificity and diversity for these important enzymes to control the properties and functions of ion channels.

Kinematic Design of Functional Nanoscale Mechanisms From Molecular Primitives

2020 ◽  
Author(s):  
Pouya Tavousi ◽  
Meysam T. Chorsi ◽  
Caitlyn Mundrane ◽  
Vitaliy Gorbatyuk ◽  
Kazem Kazerounian ◽  
...  
Keyword(s):  
Ion Channels ◽  
Range Of Motion ◽  
Systematic Approach ◽  
Design Space ◽  
Vital Role ◽  
Degree Of Freedom ◽  
Living Systems ◽  
Kinematic Design ◽  
Systematic Exploration ◽  
And Function

Abstract Natural nanomechanisms such as capillaries, neurotransmitters, and ion channels play a vital role in the living systems. But the design principles developed by nature through evolution are not well understood and, hence, not applicable to engineered nanomachines. Thus, the design of nanoscale mechanisms with prescribed functions remains a challenge. Here, we present a systematic approach based on established kinematics techniques to designing, analyzing, and controlling manufacturable nanomachines with prescribed mobility and function built from a finite but extendable number of available “molecular primitives.” Our framework allows the systematic exploration of the design space of irreducibly simple nanomachines, built with prescribed motion specification by combining available nanocomponents into systems having constrained, and consequently controllable motions. We show that the proposed framework has allowed us to discover and verify a molecule in the form of a seven link, seven revolute (7R) close loop spatial linkage with mobility (degree of freedom) of one. Furthermore, our experiments exhibit the type and range of motion predicted by our simulations. Enhancing such a structure into functional nanomechanisms by exploiting and controlling their motions individually or as part of an ensemble could galvanize development of the multitude of engineering, scientific, medical, and consumer applications that can benefit from engineered nanomachines.

Calcium-Permeable Ion Channels in Pain Signaling

2014 ◽  
Vol 94 (1) ◽  
pp. 81-140 ◽  
Author(s):  
Emmanuel Bourinet ◽  
Christophe Altier ◽  
Michael E. Hildebrand ◽  
Tuan Trang ◽  
Michael W. Salter ◽  
...  
Keyword(s):  
Ion Channels ◽  
Trp Channels ◽  
Neuronal Firing ◽  
Spinal Cord Neurons ◽  
Wide Range ◽  
Pain Pathway ◽  
Channel Expression ◽  
And Function ◽  
The Brain

The detection and processing of painful stimuli in afferent sensory neurons is critically dependent on a wide range of different types of voltage- and ligand-gated ion channels, including sodium, calcium, and TRP channels, to name a few. The functions of these channels include the detection of mechanical and chemical insults, the generation of action potentials and regulation of neuronal firing patterns, the initiation of neurotransmitter release at dorsal horn synapses, and the ensuing activation of spinal cord neurons that project to pain centers in the brain. Long-term changes in ion channel expression and function are thought to contribute to chronic pain states. Many of the channels involved in the afferent pain pathway are permeable to calcium ions, suggesting a role in cell signaling beyond the mere generation of electrical activity. In this article, we provide a broad overview of different calcium-permeable ion channels in the afferent pain pathway and their role in pain pathophysiology.

Probing Structure and Function of Ion Channels Using Limited Proteolysis and Microfluidics

2014 ◽  
Vol 136 (42) ◽  
pp. 14875-14882 ◽  
Author(s):  
Carolina L. Trkulja ◽  
Erik T. Jansson ◽  
Kent Jardemark ◽  
Owe Orwar
Keyword(s):  
Ion Channels ◽  
Limited Proteolysis ◽  
Structure And Function ◽  
And Function
Sign in / Sign up

Export Citation Format

Share Document