Key Amino Acid Residues of Ankyrin-Sensitive Phosphatidylethanolamine/Phosphatidylcholine-Lipid Binding Site of βI-Spectrin

It was shown previously that an ankyrin-sensitive, phosphatidylethanolamine/phosphatidylcholine (PE/PC) binding site maps to the N-terminal part of the ankyrin-binding domain of β-spectrin (ankBDn). Here we have identified the amino acid residues within this domain which are responsible for recognizing monolayers and bilayers composed of PE/PC mixtures. In vitro binding studies revealed that a quadruple mutant with substituted hydrophobic residues W1771, L1775, M1778 and W1779 not only failed to effectively bind PE/PC, but its residual PE/PC-binding activity was insensitive to inhibition with ankyrin. Structure prediction and analysis, supported by in vitro experiments, suggests that “opening” of the coiled-coil structure underlies the mechanism of this interaction. Experiments on red blood cells and HeLa cells supported the conclusions derived from the model and in vitro lipid-protein interaction results, and showed the potential physiological role of this binding. We postulate that direct interactions between spectrin ankBDn and PE-rich domains play an important role in stabilizing the structure of the spectrin-based membrane skeleton

The drainage pattern of Hansbreen and Werenskioldbreen, two polythermal glaciers in Svalbard

To improve our understanding of Svalbard-type polythermal glacier drainage, hydraulic geometry models of the subglacial hydrology of two contrasting glaciers in Svalbard have been constructed. The models are tested against a uniquely long and rich set of field observations spanning 45 years. Digital elevation models (DEMs) were constructed from bedrock data measured with ground penetrating radar and surface data of two medium-sized polythermal glaciers, Hansbreen and Werenskioldbreen, in south-west Spitsbergen. Hansbreen has a low angle bed with over-deepenings and a calving front, while Werenskioldbreen has steeper bed and terminates on land. Together they are representative of many Svalbard glaciers. The DEMs were used to derive maps of hydraulic potential and subglacial drainage networks. Validation of the models was done using field observations including location mapping and speleological exploration of active moulins, positions of main river outflows, dyetracing and water chemistry studies, and observations of water pressure inside moulins. Results suggest that the water pressure is generally close to ice overburden pressure but varies greatly depending on local conditions such as bed location, the thickness of cold ice layer, the thickness of the glacier and seasonal changes in meltwater input

The role of hydrophobic interactions in ankyrin-spectrin complex formation

Spectrin and ankyrin are the key components of the erythrocyte cytoskeleton. The recently published crystal structure of the spectrin-ankyrin complex has indicated that their binding involves complementary charge interactions as well as hydrophobic interactions. However, only the former is supported by biochemical evidence. We now show that nonpolar interactions are important for high affinity complex formation, excluding the possibility that the binding is exclusively mediated by association of distinctly charged surfaces. Along these lines we report that substitution of a single hydrophobic residue, F917S in ankyrin, disrupts the structure of the binding site and leads to complete loss of spectrin affinity. Finally, we present data showing that minimal ankyrin binding site in spectrin is formed by helix 14C together with the loop between helices 15 B/C

Key Amino Acid Residues of Ankyrin-Sensitive Phosphatidylethanolamine/Phosphatidylcholine-Lipid Binding Site of beta I-Spectrin

It was shown previously that an ankyrin-sensitive, phosphatidylethanolamine/phosphatidylcholine (PE/PC) binding site maps to the N-terminal part of the ankyrin-binding domain of β-spectrin (ankBDn). Here we have identified the amino acid residues within this domain which are responsible for recognizing monolayers and bilayers composed of PE/PC mixtures. In vitro binding studies revealed that a quadruple mutant with substituted hydrophobic residues W1771, L1775, M1778 and W1779 not only failed to effectively bind PE/PC, but its residual PE/PC-binding activity was insensitive to inhibition with ankyrin. Structure prediction and analysis, supported by in vitro experiments, suggests that "opening" of the coiled-coil structure underlies the mechanism of this interaction. Experiments on red blood cells and HeLa cells supported the conclusions derived from the model and in vitro lipid-protein interaction results, and showed the potential physiological role of this binding. We postulate that direct interactions between spectrin ankBDn and PE-rich domains play an important role in stabilizing the structure of the spectrin-based membrane skeleton

Geodetic and satellite derived ice surface velocities of Vestfonna ice cap

During 2007 we launched a geodetic campaign on the Svalbard ice cap Vestfonna in order to estimate the velocity field of the ice cap. This was done within the frame of the IPY project KINNVIKA. We present here the velocity measurements derived from our campaigns 2007-2010 and compare the geodetic measurements against InSAR velocity fields from satellite platforms from 1995/96 and 2008. We find the spatial distribution of ice speeds from the InSAR is in good agreement within the uncertainty limits with our geodetic measurements. We observe no clear indication of seasonal ice speed differences, but we find a speed-up of the outlet glacier Franklinbreen between the InSAR campaigns, and speculate the outlet is having a surge phase