KCNKØ: opening and closing the 2-P-domain potassium leak channel entails "C-type" gating of the outer pore.

Essential to nerve and muscle function, little is known about how potassium leak channels operate. KCNKØ opens and closes in a kinase-dependent fashion. Here, the transition is shown to correspond to changes in the outer aspect of the ion conduction pore. Voltage-gated potassium (VGK) channels open and close via an internal gate; however, they also have an outer pore gate that produces "C-type" inactivation. While KCNKØ does not inactivate, KCNKØ and VGK channels respond in like manner to outer pore blockers, potassium, mutations, and chemical modifiers. Structural relatedness is confirmed: VGK residues that come close during C-type gating predict KCNKØ sites that crosslink (after mutation to cysteine) to yield channels controlled by reduction and oxidization. We conclude that similar outer pore gates mediate KCNKØ opening and closing and VGK channel C-type inactivation despite their divergent structures and physiological roles

Charge sensing amplification via weak values measurement

A protocol employing weak values (WVs) to obtain ultra sensitive amplification of weak signals in the context of a solid state setup is proposed. We consider an Aharonov-Bohm interferometer where both the orbital and the spin degrees of freedom are weakly affected by the presence of an external charge to be detected. The interplay between the spin and the orbital WVs leads to a significant amplification even in the presence of finite temperature, voltage, and external noise.Comment: 6 pages, 5 figure

Block of Kcnk3 by protons. Evidence that 2-P-domain potassium channel subunits function as homodimers.

KCNK subunits have two pore-forming P domains and four predicted transmembrane segments. To assess the number of subunits in each pore, we studied external proton block of Kcnk3, a subunit prominent in rodent heart and brain. Consistent with a pore-blocking mechanism, inhibition was dependent on voltage, potassium concentration, and a histidine in the first P domain (P1H). Thus, at pH 6.8 with 20 mm potassium half the current passed by P1H channels was blocked (apparently via two sites approximately 10% into the electrical field) whereas channels with an asparagine substitution (P1N) were fully active. Furthermore, pore blockade by barium was sensitive to pH in P1H but not P1N channels. Although linking two Kcnk3 subunits in tandem to produce P1H-P1H and P1N-P1N channels bearing four P domains did not alter these attributes, the mixed tandems P1H-P1N and P1N-P1H were half-blocked at pH approximately 6.4, apparently via a single site. This implicates a dimeric structure for Kcnk3 channels with two (and only two) P1 domains in each pore and argues that P2 domains also contribute to pore formation

Measuring cotunneling in its wake

We introduce a rate formalism to treat classically forbidden electron transport through a quantum dot (cotunneling) in the presence of a coupled measurement device. We demonstrate this formalism for a toy model case of cotunneling through a single-level dot while being coupled to a strongly pinched-off quantum point contact (QPC). We find that the detector generates three types of back-action: the measurement collapses the coherent transport through the virtual state, but at the same time allows for QPC-assisted incoherent transport, and widens the dot level. Last, we obtain the measured cotunneling time from the cross correlation between dot and QPC currents.Comment: 15 pages, 9 figures, 1 appendix, published versio