Genetic mapping of the voltage-gated shaker potassium channel beta subunit Kcnab1 to mouse Chromosome 3

1998 ◽  
Vol 9 (3) ◽  
pp. 260-260 ◽  
Author(s):  
J. M. Jones ◽  
E. Bentley ◽  
M. H. Meisler ◽  
Susan M. Darling
1996 ◽  
Vol 7 (5) ◽  
pp. 394-395 ◽  
Author(s):  
P. A. Schweitzer ◽  
N. Noben-Trauth ◽  
S. C. Pelsue ◽  
K. R. Johnson ◽  
S. F. Wolf ◽  
...  

2020 ◽  
Author(s):  
Michael F. Priest ◽  
Elizabeth E.L. Lee ◽  
Francisco Bezanilla

AbstractPositively-charged amino acids respond to membrane potential changes to drive voltage sensor movement in voltage-gated ion channels, but determining the trajectory of voltage sensor gating charges has proven difficult. We optically tracked the movement of the two most extracellular charged residues (R1, R2) in the Shaker potassium channel voltage sensor using a fluorescent positively-charged bimane derivative (qBBr) that is strongly quenched by tryptophan. By individually mutating residues to tryptophan within the putative trajectory of gating charges, we observed that the charge pathway during activation is a rotation and a tilted translation that differs between R1 and R2 and is distinct from their deactivation pathway. Tryptophan-induced quenching of qBBr also indicates that a crucial residue of the hydrophobic plug is linked to the Cole-Moore shift through its interaction with R1. Finally, we show that this approach extends to additional voltage-sensing membrane proteins using the Ciona intestinalis voltage sensitive phosphatase (CiVSP).


eLife ◽  
2021 ◽  
Vol 10 ◽  
Author(s):  
Michael F Priest ◽  
Elizabeth EL Lee ◽  
Francisco Bezanilla

Positively-charged amino acids respond to membrane potential changes to drive voltage sensor movement in voltage-gated ion channels, but determining the displacements of voltage sensor gating charges has proven difficult. We optically tracked the movement of the two most extracellular charged residues (R1, R2) in the Shaker potassium channel voltage sensor using a fluorescent positively-charged bimane derivative (qBBr) that is strongly quenched by tryptophan. By individually mutating residues to tryptophan within the putative pathway of gating charges, we observed that the charge motion during activation is a rotation and a tilted translation that differs between R1 and R2. Tryptophan-induced quenching of qBBr also indicates that a crucial residue of the hydrophobic plug is linked to the Cole-Moore shift through its interaction with R1. Finally, we show that this approach extends to additional voltage-sensing membrane proteins using the Ciona intestinalis voltage sensitive phosphatase (CiVSP) (Murata et al., 2005a).


Genomics ◽  
1995 ◽  
Vol 29 (3) ◽  
pp. 815-816
Author(s):  
Nandita A. Quaderi ◽  
Fernando Gianfrancesco ◽  
Steve D.M. Brown ◽  
Michele D'Urso ◽  
Maurizio D'Esposito

1998 ◽  
Vol 9 (1) ◽  
pp. 90-91 ◽  
Author(s):  
Vishnu S. Mishra ◽  
Sandra M. Holt ◽  
Juan M. Teodoro ◽  
Stephen F. Kingsmore

2010 ◽  
Vol 136 (6) ◽  
pp. 629-644 ◽  
Author(s):  
L. Revell Phillips ◽  
Kenton J. Swartz

The four voltage sensors in voltage-gated potassium (Kv) channels activate upon membrane depolarization and open the pore. The location and motion of the voltage-sensing S4 helix during the early activation steps and the final opening transition are unresolved. We studied Zn2+ bridges between two introduced His residues in Shaker Kv channels: one in the R1 position at the outer end of the S4 helix (R362H), and another in the S5 helix of the pore domain (A419H or F416H). Zn2+ bridges readily form between R362H and A419H in open channels after the S4 helix has undergone its final motion. In contrast, a distinct bridge forms between R362H and F416H after early S4 activation, but before the final S4 motion. Both bridges form rapidly, providing constraints on the average position of S4 relative to the pore. These results demonstrate that the outer ends of S4 and S5 remain in close proximity during the final opening transition, with the S4 helix translating a significant distance normal to the membrane plane.


1995 ◽  
Vol 6 (5) ◽  
pp. 378-379
Author(s):  
S. F. Kingsmore ◽  
A. P. Spicer ◽  
S. J. Gendler ◽  
M. F. Seldin

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