Double Star TC-1 observation of the earthward flowing plasmoids in the near magnetotail

We analyze Double Star TC-1 magnetic field data from July to September in 2004 and find that plas-moids exist in the very near-Earth magnetotail. It is the first time that TC-1 observes the plasmoids inthe magnetotail at X > ?13 RE. According to the difference of the magnetic field structure in plasmoids,we choose two typical cases for our study: the magnetic flux rope on August 6 with the open magneticfield and the magnetic loop on September 14 with the closed magnetic field. Both of the cases are as-sociated with the high speed earthward flow and the magnetic loop is related to a strong substorm. Theions can escape from the magnetic flux rope along its open field line, but the case of the closed mag-netic loop can trap the ions. The earthward flowing plasmoids observed by TC-1 indicate that the mul-tiple X-line magnetic reconnection occurs beyond the distance of X=?10 RE from the earth.     

Groundwater formation of martian valleys

The martian surface shows large outflow channels, widely accepted as having been formed by gigantic floods that could have occurred under climatic conditions like those seen today. Also present are branching valley networks that commonly have tributaries. These valleys are much smaller than the outflow channels and their origins and ages have been controversial. For example, they might have formed through slow erosion by water running across the surface, either early or late in Mars' history, possibly protected from harsh conditions by ice cover. Alternatively, they might have formed through groundwater or ground-ice processes that undermine the surface and cause collapse, again either early or late in Mars' history. Long-duration surface runoff would imply climatic conditions quite different from the present environment. Here we present high-resolution images of martian valleys that support the view that ground water played an important role in their formation, although we are unable as yet to establish when this occurred.     

Structural basis for AMP binding to mammalian AMP-activated protein kinase

AMP-activated protein kinase (AMPK) regulates cellular metabolism in response to the availability of energy and is therefore a target for type II diabetes treatment. It senses changes in the ratio of AMP/ATP by binding both species in a competitive manner. Thus, increases in the concentration of AMP activate AMPK resulting in the phosphorylation and differential regulation of a series of downstream targets that control anabolic and catabolic pathways. We report here the crystal structure of the regulatory fragment of mammalian AMPK in complexes with AMP and ATP. The phosphate groups of AMP/ATP lie in a groove on the surface of the gamma domain, which is lined with basic residues, many of which are associated with disease-causing mutations. Structural and solution studies reveal that two sites on the gamma domain bind either AMP or Mg.ATP, whereas a third site contains a tightly bound AMP that does not exchange. Our binding studies indicate that under physiological conditions AMPK mainly exists in its inactive form in complex with Mg.ATP, which is much more abundant than AMP. Our modelling studies suggest how changes in the concentration of AMP ([AMP]) enhance AMPK activity levels. The structure also suggests a mechanism for propagating AMP/ATP signalling whereby a phosphorylated residue from the alpha and/or beta subunits binds to the gamma subunit in the presence of AMP but not when ATP is bound.     

Sensory neuron sodium channel Nav1.8 is essential for pain at low temperatures

Sensory acuity and motor dexterity deteriorate when human limbs cool down, but pain perception persists and cold-induced pain can become excruciating. Evolutionary pressure to enforce protective behaviour requires that damage-sensing neurons (nociceptors) continue to function at low temperatures. Here we show that this goal is achieved by endowing superficial endings of slowly conducting nociceptive fibres with the tetrodotoxin-resistant voltage-gated sodium channel (VGSC) Na(v)1.8 (ref. 2). This channel is essential for sustained excitability of nociceptors when the skin is cooled. We show that cooling excitable membranes progressively enhances the voltage-dependent slow inactivation of tetrodotoxin-sensitive VGSCs. In contrast, the inactivation properties of Na(v)1.8 are entirely cold-resistant. Moreover, low temperatures decrease the activation threshold of the sodium currents and increase the membrane resistance, augmenting the voltage change caused by any membrane current. Thus, in the cold, Na(v)1.8 remains available as the sole electrical impulse generator in nociceptors that transmits nociceptive information to the central nervous system. Consistent with this concept is the observation that Na(v)1.8-null mutant mice show negligible responses to noxious cold and mechanical stimulation at low temperatures. Our data present strong evidence for a specialized role of Na(v)1.8 in nociceptors as the critical molecule for the perception of cold pain and pain in the cold.