| Nerve ending "signal" proteins GAP-43, MARCKS, and BASP1. | |
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MedLine Citation:
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PMID: 16125549 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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Mechanisms of growth cone pathfinding in the course of neuronal net formation as well as mechanisms of learning and memory have been under intense investigation for the past 20 years, but many aspects of these phenomena remain unresolved and even mysterious. "Signal" proteins accumulated mainly in the axon endings (growth cones and the presynaptic area of synapses) participate in the main brain processes. These proteins are similar in several essential structural and functional properties. The most prominent similarities are N-terminal fatty acylation and the presence of an "effector domain" (ED) that dynamically binds to the plasma membrane, to calmodulin, and to actin fibrils. Reversible phosphorylation of ED by protein kinase C modulates these interactions. However, together with similarities, there are significant differences among the proteins, such as different conditions (Ca2+ contents) for calmodulin binding and different modes of interaction with the actin cytoskeleton. In light of these facts, we consider GAP-43, MARCKS, and BASP1 both separately and in conjunction. Special attention is devoted to a discussion of apparent inconsistencies in results and opinions of different authors concerning specific questions about the structure of proteins and their interactions. |
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Authors:
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Mark I Mosevitsky |
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Publication Detail:
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Type: Journal Article; Research Support, Non-U.S. Gov't; Review |
Journal Detail:
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Title: International review of cytology Volume: 245 ISSN: 0074-7696 ISO Abbreviation: Int. Rev. Cytol. Publication Date: 2005 |
Date Detail:
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Created Date: 2005-08-29 Completed Date: 2006-02-22 Revised Date: 2006-11-15 |
Medline Journal Info:
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Nlm Unique ID: 2985180R Medline TA: Int Rev Cytol Country: United States |
Other Details:
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Languages: eng Pagination: 245-325 Citation Subset: IM |
Affiliation:
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Division of Molecular and Radiation Biophysics, Petersburg Nuclear Physics Institute, Russian Academy of Sciences, 188300 Gatchina Leningrad District, Russian Federation. |
Export Citation:
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APA/MLA Format Download EndNote Download BibTex |
| MeSH Terms | |
Descriptor/Qualifier:
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Animals Calmodulin-Binding Proteins / physiology* Cytoskeletal Proteins / physiology* GAP-43 Protein / physiology* Humans Intracellular Signaling Peptides and Proteins / physiology* Membrane Proteins / physiology* Nerve Endings / physiology* Nerve Tissue Proteins / physiology* Repressor Proteins / physiology* |
| Chemical | |
Reg. No./Substance:
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0/BASP1 protein, human; 0/Basp1 protein, mouse; 0/Calmodulin-Binding Proteins; 0/Cytoskeletal Proteins; 0/GAP-43 Protein; 0/Intracellular Signaling Peptides and Proteins; 0/Membrane Proteins; 0/Nerve Tissue Proteins; 0/Repressor Proteins; 125267-21-2/myristoylated alanine-rich C kinase substrate; 131553-58-7/Basp1 protein, rat |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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