Fc receptor phosphorylation during receptor-mediated control of B-cell activation
Article Abstract:
An important but poorly understood aspect of cell function is how receptor molecules on the cell surface respond to contact by specific substances and trigger the stimulation of events within the cell. Within the immune system, several cell types have receptors which bind complexes of antibodies and antigens. Since these receptors bind to the constant fragment of the antibody, rather than to the variable region which sticks to the antigen, they are called Fc receptors. Investigators are now examining the mechanisms by which the Fc receptors stimulate events within the cell and have discovered that different types of Fc receptors, called isoforms, may work by different mechanisms. They found that the FcRII-B1 isoform has an extra 47 amino acids in its tail. These extra amino acids provide sites for phosphorylation, sites that are missing from the FcRII-B2 isoform. Phosphorylation is the adding of phosphate to certain spots on the protein, and is widely thought to be an important part of regulating protein function within the cell. The B1 isoform is found on B-cells, while the B2 isoform is found on macrophages. Both cell types are an important part of the immune system, and both types respond to antibodies. In addition, both cell types use their Fc receptors to initiate this response. However, since the cells respond in different ways to the same stimulus, the differences in the Fc receptors may be responsible for eliciting different reactions. (Consumer Summary produced by Reliance Medical Information, Inc.)
Publication Name: Nature
Subject: Zoology and wildlife conservation
ISSN: 0028-0836
Year: 1990
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A diffusion barrier maintains distribution of membrane proteins in polarized neurons
Article Abstract:
Some membrane proteins are shown to have markedly reduced mobility in the initial segment of the axon. The diffusion barrier is abolished with disruption of F-actin and low dimethyl sulphoxide (DMSO) levels, resulting in redistribution of membrane markers that were previously polarized. Immobilization may reflect differential tethering to cytoskeletal components.
Publication Name: Nature
Subject: Zoology and wildlife conservation
ISSN: 0028-0836
Year: 1999
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Setting logical priorities
Article Abstract:
Issues surrounding moves towards the free exchange of scientific information are discussed. Particular focus is given to the Public Library of Science's threat to boycott scientific journals.
Publication Name: Nature
Subject: Zoology and wildlife conservation
ISSN: 0028-0836
Year: 2001
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