G protein heterodimers: new structures propel new questions

Article Abstract:

Recent studies that have elucidated the structure of G proteins are bound to stimulate further researches as to the functions posed by these structures. Some interesting structural questions are the single cleavage site in the beta subunit despite the presence of several potential sites which may have to do with the way with which the loop exposes the site. Another is the use of WD repeats (amino acid sequences bounded by Trp-Asp) to form the propeller configuration, and the function of the propeller configuration.

author: Neer, Eva J., Smith, Temple F.
Proteins, G proteins, Protein structure

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Mechanism by which Liddle's syndrome mutations increase activity of a human epithelial Na+ channel

Article Abstract:

Liddle's syndrome is due to mutations in the C-terminal of the human epithelial Na+ channel (hENaC) subunits which causes hypertension by increasing Na+ absorption. The increased Na+ absorption is due to an increase in the number of Na+ channels in the epithelium. The conductance of individual channels is unaltered. The mutation is the deletion of conserved sequences in the C-terminal which control the internalization of hENaC.

author: Price, Margaret P., Welsh, Michael J., Adams, Christopher M., Snyder, Peter M., McDonald, Fiona J., Volk, Kenneth A., Zeiher, Bernhardt G., Stokes, John B.
Abnormalities, Hypertension, Causes of, Physiological aspects, Epithelial cells, Mutation (Biology), Mutation, Dyskeratosis congenita

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Structure and function of the beta-2 subunit of brain sodium channels, a transmembrane glycoprotein with a CAM motif

Article Abstract:

The beta-2 subunits of voltage-gated sodium channels play a major role in the regulation of sodium channel expression in neurons. A study of cDNA cloning and sequencing of the beta-2 subunit indicates the presence of a 186 residue glycoprotein with an extracellular NH2-terminal region. The region has an immunoglobulin-like fold, with resemblance to contactin, a small intracellular domain and a single transmembrane segment.

author: Isom, L.L., Ragsdale, D.S., De Jongh, K.S., Westenbroek, R.E., Reber, B.F.X., Scheuer, T., Catterall, W.A.
Observations, Cloning

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subjects list: Research, Analysis, Amino acid sequence, Amino acid sequencing, Sodium channels
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