Surface velocity and ice discharge of the ice cap on King George Island, Antarctica

Glaciers on King George Island, Antarctica, have shown retreat and surface lowering in recent decades, concurrent with increasing air temperatures. A large portion of the glacier perimeter is ocean-terminating, suggesting possible large mass losses due to calving and submarine melting. Here we estimate the ice discharge into the ocean for the King George Island ice cap. L-band synthetic aperture radar images covering the time-span January 2008 to January 2011 over King George Island are processed using an intensity-tracking algorithm to obtain surface velocity measurements. Pixel offsets from 40 pairs of radar images are analysed and inverted to estimate a weighted average surface velocity field. Ice thicknesses are derived from simple principles of ice flow mechanics using the computed surface velocity fields and in situ thickness data. The maximum ice surface speeds reach mayor que 225 m/yr, and the total ice discharge for the analysed flux gates of King George Island is estimated to be 0.720+/-0.428 Gt/yr, corresponding to a specific mass loss of 0.64+/-0.38 m w.e./yr over the area of the entire ice cap (1127 km2).

A history of the British zoophytes. By George Johnston.

2, Plates

A history of the British zoophytes. By George Johnston.

1, Text

Narrative of the voyage of H.M.S. Rattlesnake, commanded by the late Captain Owen Stanley during the years 1846-50, including discoveries and surveys in New Guinea, the Louisiade Archipelago, etc : to which is added Mr. E.B. Kennedy's expedition for the exploration of the Cape York Peninsula / by John Macgillivray.

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The conserved SOCS box motif in suppressors of cytokine signaling binds to elongins B and C and may couple bound proteins to proteasomal degradation

The suppressors of cytokine signaling (SOCS) family of proteins act as intracellular inhibitors of several cytokine signal transduction pathways. Their expression is induced by cytokine activation of the Janus kinase/signal transducer and activator of transcription (JAK/STAT) pathway and they act as a negative feedback loop by subsequently inhibiting the JAK/STAT pathway either by direct interaction with activated JAKs or with the receptors. These interactions are mediated at least in part by the SH2 domain of SOCS proteins but these proteins also contain a highly conserved C-terminal homology domain termed the SOCS box. Here we show that the SOCS box mediates interactions with elongins B and C, which in turn may couple SOCS proteins and their substrates to the proteasomal protein degradation pathway. Analogous to the family of F-box-containing proteins, it appears that the SOCS proteins may act as adaptor molecules that target activated cell signaling proteins to the protein degradation pathway.

Act1, an NF-κB-activating protein

Use of an NF-κB-dependent selectable marker facilitated the isolation of a cell line containing a cDNA encoding Act1, an NF-κB activator. Act1 associates with and activates IκB kinase (IKK), leading to the liberation of NF-κB from its complex with IκB. Many signaling pathways that liberate NF-κB also activate activating transcription factor (ATF) and activator protein 1 (AP-1) through Jun kinase (JNK). Act1 also activates JNK, suggesting that it might be part of a multifunctional complex involved in the activation of both NF-κB and JNK. Act1 fails to activate NF-κB in an IL-1-unresponsive mutant cell line in which all known signaling components are present, suggesting that it interacts with an unknown component in IL-1 signaling.

IL-1-induced NFκB and c-Jun N-terminal kinase (JNK) activation diverge at IL-1 receptor-associated kinase (IRAK)

Mutant I1A cells, lacking IL-1 receptor-associated kinase (IRAK) mRNA and protein, have been used to study the involvement of IRAK in NFκB and c-Jun N-terminal kinase (JNK) activation. A series of IRAK deletion constructs were expressed in I1A cells, which were then tested for their ability to respond to IL-1. Both the N-terminal death domain and the C-terminal region of IRAK are required for IL-1-induced NFκB and JNK activation, whereas the N-proximal undetermined domain is required for the activation of NFκB but not JNK. The phosphorylation and ubiquitination of IRAK deletion mutants correlate tightly with their ability to activate NFκB in response to IL-1, but IRAK can mediate IL-1-induced JNK activation without being phosphorylated. These studies reveal that the IL-1-induced signaling pathways leading to NFκB and JNK activation diverge either at IRAK or at a point nearer to the receptor.