February 2016 | Volume 147, No. 2
- Currents through Hv1 channels deplete protons in their vicinity
The pH-sensitive fluorescent protein Venus can be used as an optical reporter for proton flux when fused to an intracellular domain of Hv1 channels.
- Orai1 pore residues control CRAC channel inactivation independently of calmodulin
Researchers have reevaluated the role of calmodulin and previously identified calmodulin binding sites in the mechanism by which Ca2+-release activated Ca2+ channels can be inactivated as Ca2+ ions enter cells.
- The inactivation domain of STIM1 is functionally coupled with the Orai1 pore to enable Ca2+-dependent inactivation
Researchers examined the role of a domain within the stromal interaction molecule (STIM) in the mechanism by which Ca2+ release–activated Ca2+ channels can be inactivated as Ca2+ ions enter cells.
- Carbenoxolone inhibits Pannexin1 channels through interactions in the first extracellular loop
A chimeric approach combined with extensive site-directed mutagenesis reveals new information about the interaction of the toxin carbenoxolone with the ATP release channel Pannexin1 and the role of the first extracellular loop in channel gating.
- Distinct α2 Na,K-ATPase membrane pools are differently involved in early skeletal muscle remodeling during disuse
Location, location, location. The Na-K pump of skeletal muscle is regulated differently at neuromuscular junctions.
Methods and Approaches
- Transition metal ion FRET to measure short-range distances at the intracellular surface of the plasma membrane
A novel method is presented to measure short distances in cell plasma membranes using transition metal ion FRET with metal ions bound to introduced sites in the membrane.
- Measuring distances between TRPV1 and the plasma membrane using a noncanonical amino acid and transition metal ion FRET
Transition metal ion FRET between a noncanonical fluorescent amino acid incorporated into TRPV1 and metal ions bound to the cell plasma can be used to measure distances and dynamics between cytosolic domains of proteins and the membrane.