An international gathering of physiologists in Valparaiso, Chile.

The June issue of is a collection of peer-reviewed articles contributed by participants of the very special Society of General Physiologists (SGP) 73rd Annual Symposium, hosted jointly with the Society of Latin American Biophysicists (SOBLA).

Dynamic response of model lipid membranes to ultrasonic radiation force.

Low-intensity ultrasound can modulate action potential firing in neurons in vitro and in vivo. It has been suggested that this effect is mediated by mechanical interactions of ultrasound with neural cell membranes. We investigated whether these proposed interactions could be reproduced for further study in a synthetic lipid bilayer system.

A designed inhibitor of a CLC antiporter blocks function through a unique binding mode.

The lack of small-molecule inhibitors for anion-selective transporters and channels has impeded our understanding of the complex mechanisms that underlie ion passage. The ubiquitous CLC "Chloride Channel" family represents a unique target for biophysical and biochemical studies because its distinctive protein fold supports both passive chloride channels and secondary-active chloride-proton transporters. Here, we describe the synthesis and characterization of a specific small-molecule inhibitor directed against a CLC antiporter (ClC-ec1).

Biochemistry to the rescue: a ClC-2 auxiliary subunit provides a tangible link to leukodystrophy.

ClC-2 is a broadly distributed chloride channel with an enigmatic neurophysiological function. In this issue of Neuron, Jeworutzki et al. (2012) use a biochemical approach to identify GlialCAM, a protein with a defined link to leukodystrophy, as a ClC-2 auxiliary subunit.

Substrate-driven conformational changes in ClC-ec1 observed by fluorine NMR.

The CLC 'Cl(-) channel' family consists of both Cl(-)/H(+) antiporters and Cl(-) channels. Although CLC channels can undergo large, conformational changes involving cooperativity between the two protein subunits, it has been hypothesized that conformational changes in the antiporters may be limited to small movements localized near the Cl(-) permeation pathway. However, to date few studies have directly addressed this issue, and therefore little is known about the molecular movements that underlie CLC-mediated antiport.