The ninth annual Ion Channel Retreat, Vancouver, Canada, June 27-29, 2011.

Nine years ago Aurora Biomed Inc. (Vancouver, Canada) committed to gathering the brightest minds and the most innovative research companies at one conference. The Ion Channel Retreat provides a podium for scientific discourse spanning a wide range of ion channel disciplines. This conference has consistently provided a venue for people to share knowledge, exchange ideas, and establish partnerships. This conference continues to expand and grow each year, demonstrating the value of such a conference. Attendees at the 2011 Ion Channel retreat presented ion channel research from 12 different countries, representing research groups located on 5 of the 7 continents. Aurora Biomed's 2011 Retreat covered a variety of topics including Ion Channels as Disease Targets, Ion Channels as Pain Targets, TRP-channels, Ion Channel Screening Technologies, Cardiac Function and Pharmacology, Cardiac Safety and Toxicology, and Structure and Function of Ion Channels.

Nemo phosphorylates Even-skipped and promotes Eve-mediated repression of odd-skipped in even parasegments during Drosophila embryogenesis.

Drosophila nemo (nmo) and other Nemo-like kinase family members (Nlks) are well-established key regulators of numerous conserved signaling pathways, such as Wg and BMP. nmo mutants display pleiotropic defects at different developmental stages, including the embryo. In this study we describe a detailed characterization of embryonic cuticle patterning defects associated with maternal loss of nmo. nmo mutant embryos consistently show segmentation defects, most frequently fusions of pairs of denticle belts in alternating segments. These phenotypes are reminiscent of those associated with defects in pair-rule patterning. Genetic interaction studies demonstrate that Nmo promotes Even-skipped (Eve) activity and is required to promote the expression of the Eve target, engrailed (en), in even numbered parasegments. We find that Nmo regulates a subset of Eve activities by stimulating Eve-mediated suppression of the odd-skipped (odd) repressor. Furthermore, we isolate Nmo in a protein complex with Eve and show that Nmo phosphorylates Eve in in vitro kinase assays. These studies reveal a novel role for the Nmo kinase in embryonic pattern formation through its regulation of the homeodomain-containing transcription factor Eve.