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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
2
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pubmed:dateCreated |
1992-6-2
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pubmed:abstractText |
The ATP.Mg-dependent type-1 protein phosphatase activating factor (FA) was identified as a protein kinase that could phosphorylate synapsin I, a neuronal protein that coats synaptic vesicles, binds to cytoskeleton and is believed to be involved in the modulation of neurotransmission. More importantly, more than 90% of the phosphates in 32P-synapsin I phosphorylated by FA could be removed by the activated ATP.Mg-dependent type-1 protein phosphatase and the synapsin I phosphatase activity was found to be strictly FA-dependent. Functional study further revealed that as a synapsin I kinase, factor FA could phosphorylate synapsin I and thereby inhibits crosslinking of synapsin I with tubulin, while as a synapsin I phosphatase activator, FA could promote the crosslinking copolymerization of synapsin I with tubulin. Taken together, the results provide initial evidence that a cyclic modulation of the crosslinking copolymerization of synapsin I with brain microtubules can be controlled by factor FA, representing an efficient cyclic cascade control mechanism for the regulation of axonal transport process during neurotransmission.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Calcium-Calmodulin-Dependent...,
http://linkedlifedata.com/resource/pubmed/chemical/Cross-Linking Reagents,
http://linkedlifedata.com/resource/pubmed/chemical/Phosphorylase Kinase,
http://linkedlifedata.com/resource/pubmed/chemical/Phosphorylase a,
http://linkedlifedata.com/resource/pubmed/chemical/Phosphorylase b,
http://linkedlifedata.com/resource/pubmed/chemical/Protein Kinases,
http://linkedlifedata.com/resource/pubmed/chemical/Synapsins,
http://linkedlifedata.com/resource/pubmed/chemical/Tubulin
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pubmed:status |
MEDLINE
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pubmed:month |
Apr
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pubmed:issn |
0006-291X
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
30
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pubmed:volume |
184
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
973-9
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pubmed:dateRevised |
2009-11-19
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pubmed:meshHeading |
pubmed-meshheading:1315541-Animals,
pubmed-meshheading:1315541-Brain,
pubmed-meshheading:1315541-Calcium-Calmodulin-Dependent Protein Kinases,
pubmed-meshheading:1315541-Cross-Linking Reagents,
pubmed-meshheading:1315541-Kinetics,
pubmed-meshheading:1315541-Microtubules,
pubmed-meshheading:1315541-Molecular Weight,
pubmed-meshheading:1315541-Phosphorylase Kinase,
pubmed-meshheading:1315541-Phosphorylase a,
pubmed-meshheading:1315541-Phosphorylase b,
pubmed-meshheading:1315541-Phosphorylation,
pubmed-meshheading:1315541-Protein Kinases,
pubmed-meshheading:1315541-Swine,
pubmed-meshheading:1315541-Synapsins,
pubmed-meshheading:1315541-Synaptic Vesicles,
pubmed-meshheading:1315541-Tubulin
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pubmed:year |
1992
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pubmed:articleTitle |
Cyclic inhibition-potentiation of the crosslinking of synapsin I with brain microtubules by protein kinase FA (an activator of ATP.Mg-dependent protein phosphatase).
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pubmed:affiliation |
Institute of Biomedical and Life Sciences, National Tsing Hua University, Taiwan, ROC.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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