Document Detail


Nerve ending "signal" proteins GAP-43, MARCKS, and BASP1.
MedLine Citation:
PMID:  16125549     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
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.
Authors:
Mark I Mosevitsky
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't; Review    
Journal Detail:
Title:  International review of cytology     Volume:  245     ISSN:  0074-7696     ISO Abbreviation:  Int. Rev. Cytol.     Publication Date:  2005  
Date Detail:
Created Date:  2005-08-29     Completed Date:  2006-02-22     Revised Date:  2006-11-15    
Medline Journal Info:
Nlm Unique ID:  2985180R     Medline TA:  Int Rev Cytol     Country:  United States    
Other Details:
Languages:  eng     Pagination:  245-325     Citation Subset:  IM    
Affiliation:
Division of Molecular and Radiation Biophysics, Petersburg Nuclear Physics Institute, Russian Academy of Sciences, 188300 Gatchina Leningrad District, Russian Federation.
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MeSH Terms
Descriptor/Qualifier:
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:
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

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