Chicken Growth‐Associated Protein GAP‐43 Is Tightly Bound to the Actin‐Rich Neuronal Membrane Skeleton
- 1 March 1990
- journal article
- research article
- Published by Wiley in Journal of Neurochemistry
- Vol. 54 (3), 729-736
- https://doi.org/10.1111/j.1471-4159.1990.tb02312.x
Abstract
We have identified the chicken equivalent of growth-associated protein GAP-43 in a detergent-resistant membrane skeleton from cultures of chick neurones and embryonic chick brain. Antisera to the membrane skeleton protein, the 3D5 antigen, precipitate the translocation product of chick GAP-43 cDNA, and the 3D5 antigen is also detected by antisera against synthetic peptides from the known amino acid sequence of rat GAP-43. The chick protein and the rat GAP-43 are biochemically similar proteins that both serve as major targets of phosphorylation by endogenous protein kinase C. The detergent-resistant complex in which GAP-43 is found also contains actin (.apprx. 5% of the total protein) and a neuone-specific cell surface glycoprotein. We suggest that the membrane skeleton of neurones may be a primary site of action of GAP-43.Keywords
This publication has 38 references indexed in Scilit:
- A developmentally regulated chicken neuronal protein associated with the cortical cytoskeletonJournal of Neuroscience, 1989
- Growth Cone Motility and GuidanceAnnual Review of Cell Biology, 1988
- A membrane phosphoprotein associated with neural development, axonal regeneration, phospholipid metabolism, and synaptic plasticityTrends in Neurosciences, 1987
- Primary structure and transcriptional regulation of GAP-43, a protein associated with nerve growthCell, 1987
- Molecular Properties of the Growth‐Associated Protein GAP‐43 (B‐50)Journal of Neurochemistry, 1987
- Protein kinase C phosphorylates a 47 Mr protein (F1) directly related to synaptic plasticityBrain Research, 1985
- Presynaptic localization of B-50 phosphoprotein: the (ACTH)-sensitive protein kinase substrate involved in rat brain polyphosphoinositide metabolismBrain Research, 1985
- Purification of a novel calmodulin-binding protein from bovine cerebral cortex membranesBiochemistry, 1983
- Phosphorylation of B‐50 Protein by Calcium‐Activated, Phospholipid‐Dependent Protein Kinase and B‐50 Protein KinaseJournal of Neurochemistry, 1983
- The actin content of fibroblastsBiochemical Journal, 1975