The structure of a voltage-activated potassium channel in lipid nanodiscs solved using cryo-electron microscopy is similar to previous X-ray structures, and provides insights into the mechanism of C-type inactivation.
Building on previous work (Pless, 2013), we argue that side-chain 'flip out' is a key event in potassium channel C-type inactivation, and propose a new method for encoding multiple noncanonical amino acids and controlling protein stoichiometry.
C-terminus mediated inhibition is one emerging modality of intervention for L-type Ca2+ channels, which coordinate multiple motifs to acutely tune Ca2+ current and Ca2+ influx down to the lower limits preset by end-stage Ca2+-dependent inactivation.
The ZF-CxxC protein FBXL19 recruits kinase-associated Mediator to CpG islands of silent developmental genes in embryonic stem cells, which primes these genes for activation during differentiation and is required for embryonic development.
Following fertilization, the pioneering transcription factors GAGA factor (GAF) and Zelda are independently required to reprogram the zygotic genome of Drosophila and activate the first wave of gene expression.