Polypeptide variation in an N-CAM extracellular immunoglobulin-like fold is developmentally regulated through alternative splicing

Polypeptide variation in an N-CAM extracellular immunoglobulin-like fold is developmentally regulated through alternative splicing

The alternative splicing of a previously undiscovered 30 base exon confers a new level of polypeptide diversity on the N-CAM family of cell-surface glycoproteins. It results in the insertion of 10 amino acids into the fourth of five extracellular immunoglobulin-like folds. Each major size class of r...

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Veröffentlicht in:Neuron (Cambridge, Mass.) Mass.), 1988-12, Vol.1 (10), p.1007-1017
Hauptverfasser: Small, Stephen J., Haines, Susan L., Akeson, Richard A.
Format: Artikel
Sprache:eng
Schlagworte:
Amino Acid Sequence
Amino Acids - analysis
Animals
Base Sequence
Brain - cytology
Brain - metabolism
Cell Adhesion Molecules, Neuronal - analysis
Cell Adhesion Molecules, Neuronal - genetics
Cell Adhesion Molecules, Neuronal - metabolism
Cells, Cultured
Chemical Phenomena
Chemistry
Epitopes - immunology
Exons
Gene Expression
Immunoglobulins - immunology
Molecular Sequence Data
Peptides - analysis
Peptides - immunology
Rats
RNA Splicing
RNA, Messenger - analysis
RNA, Messenger - genetics
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Zusammenfassung:The alternative splicing of a previously undiscovered 30 base exon confers a new level of polypeptide diversity on the N-CAM family of cell-surface glycoproteins. It results in the insertion of 10 amino acids into the fourth of five extracellular immunoglobulin-like folds. Each major size class of rat brain N-CAM mRNAs consists of members that contain or lack the exon. Furthermore, this splicing event is developmentally controlled: RNAs containing the inserted exon are expressed at extremely low levels (
ISSN:0896-6273
1097-4199
DOI:10.1016/0896-6273(88)90158-4