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rdf:type |
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lifeskim:mentions |
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pubmed:dateCreated |
2000-4-24
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pubmed:abstractText |
Neurofilaments comprise three subunit proteins; neurofilament light, middle and heavy chains (NF-L, NF-M and NF-H). The carboxy-terminal domains of NF-M and NF-H form side-arms that project from the filament and that of NF-H contains multiple repeats of the motif lys-ser-pro, the serines of which are targets for phosphorylation. The level of phosphorylation on the lys-ser-pro repeats varies topographically within the cell; in cell bodies and proximal axons, the side-arms are largely non-phosphorylated whereas in more distal regions of axons, the side-arms are heavily phosphorylated. Here we show that stress activated protein kinase 1b (SAPK1b), a major SAPK in neurones will phosphorylate NF-H side-arms both in vitro and in transfected cells. These studies suggest that SAPK1b targets multiple phosphorylation sites within NF-H side-arms. Additionally, we show that glutamate treatment induces activation of SAPK1b in primary cortical neurones and increased phosphorylation of NF-H in cell bodies. This suggests that glutamate causes increased NF-H phosphorylation at least in part by activation of stress activated protein kinases.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Feb
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pubmed:issn |
0021-9533
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
113 ( Pt 3)
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
401-7
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pubmed:dateRevised |
2009-11-19
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pubmed:meshHeading |
pubmed-meshheading:10639328-Animals,
pubmed-meshheading:10639328-COS Cells,
pubmed-meshheading:10639328-Cells, Cultured,
pubmed-meshheading:10639328-Cercopithecus aethiops,
pubmed-meshheading:10639328-Enzyme Activation,
pubmed-meshheading:10639328-Glutamic Acid,
pubmed-meshheading:10639328-Mitogen-Activated Protein Kinase 10,
pubmed-meshheading:10639328-Mitogen-Activated Protein Kinases,
pubmed-meshheading:10639328-Nerve Tissue Proteins,
pubmed-meshheading:10639328-Neurofilament Proteins,
pubmed-meshheading:10639328-Neurons,
pubmed-meshheading:10639328-Phosphorylation,
pubmed-meshheading:10639328-Protein Processing, Post-Translational,
pubmed-meshheading:10639328-Protein-Tyrosine Kinases,
pubmed-meshheading:10639328-Rats,
pubmed-meshheading:10639328-Recombinant Fusion Proteins,
pubmed-meshheading:10639328-Transfection
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pubmed:year |
2000
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pubmed:articleTitle |
Phosphorylation of neurofilament heavy chain side-arms by stress activated protein kinase-1b/Jun N-terminal kinase-3.
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pubmed:affiliation |
Department of Neuroscience, The Institute of Psychiatry, De Crespigny Park, Denmark Hill, London SE5 8AF, UK.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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