Ankyrin

• DOI: 10.1074/jbc.270.5.2352
• Publication Date: 2002-07-26T15:07:05Z
• Authors: Ekaterini Kordeli; Stephen Lambert; Vann Bennett
• Keywords: Ankyrins; Cerebral Cortex; 0303 health sciences; Base Sequence; Sequence Homology, Amino Acid; Molecular Sequence Data; Fluorescent Antibody Technique; Gene Expression; Nerve Tissue Proteins; Axons; Rats; Alternative Splicing; 03 medical and health sciences; Genes; Ranvier's Nodes; Animals; Humans; Tissue Distribution; Amino Acid Sequence; RNA, Messenger; Sequence Alignment

We have characterized a new ankyrin gene, expressed in brain and other tissues, that is subject to extensive tissue-specific alternative mRNA processing. The full-length polypeptide has molecular mass of 480 kDa includes predicted globular head domain, with membrane- spectrin-binding activities, as well an extended "tail" domain. term this gene ankyrinG based on its giant size general expression. Two brain-specific isoforms 270 were identified contain unique stretch sequence highly enriched serine threonine residues immediately following the Antibodies against serine-rich domain revealed labeling nodes Ranvier axonal initial segments. Ankyrin-binding proteins also known be localized these specialized membrane domains include voltage-dependent sodium channel, sodium/potassium ATPase, sodium/calcium exchanger, members neurofascin/L1 family cell adhesion molecules. neural-specific polypeptides are candidates participate maintenance/targeting ion channels molecules