Primary structure and transcriptional regulation of GAP-43, a protein associated with nerve growth.
Nerve regeneration and developmental outgrowth of axons are both correlated with increased synthesis of an axonal membrane protein designated GAP-43. Phosphorylation of an apparently identical protein, present at lower abundance in adult brains, has been correlated with long-term potentiation, a form of synaptic plasticity. We have now isolated a cDNA clone encoding GAP-43 from neonatal rat brain. The amino acid sequence is extremely hydrophilic, with no potential membrane-spanning domains and no sites for N-linked glycosylation, but with a short hydrophobic segment at the protein's amino terminus, consistent with a model in which GAP-43 extends from the cytoplasmic surface of growth cone and synaptic plasma membranes. Among several tissues and cells examined, GAP-43 mRNA is expressed only in neurons. Developmental and regeneration-associated changes in GAP-43 synthesis appear to be mediated largely at the level of transcription of a single gene.
D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D003001:Cloning, Molecular; D004247:DNA / Q000235:genetics; D019922:GAP-43 Protein; D005786:Gene Expression Regulation; D008565:Membrane Proteins / Q000235:genetics*; D009419:Nerve Tissue Proteins / Q000235:genetics*; D009474:Neurons / Q000502:physiology*; D051381:Rats; D014158:Transcription, Genetic
D019922:GAP-43 Protein; D008565:Membrane Proteins; D009419:Nerve Tissue Proteins; D004247:DNA