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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
4
|
| pubmed:dateCreated |
1998-12-30
|
| pubmed:abstractText |
The phosphorylation state of cytoskeletal proteins, including certain microtubule-associated proteins, may influence the development and plasticity of axons and dendrites in mammalian neuron in response to appropriate extracellular stimuli. In particular, high molecular weight microtubule-associated protein 2, has been implicated in dendrite growth and synaptic plasticity and is thought to be modulated by phosphorylation and dephosphorylation. We have previously determined that threonines 1620/1623 on the microtubule-associated protein 2 molecule become phosphorylated in vivo and are targets for proline-directed protein kinases in vitro. Using the phosphorylated site-specific antibody 305, we now report the decreased phosphorylation state of high molecular weight microtubule-associated protein 2 during the development of cultured cerebellar granule neurons. Phosphorylation of high molecular weight microtubule-associated protein 2 at this site is significantly inhibited by lithium in short-term cultured neurons, which suggests the implication of glycogen synthase kinase-3. In long-term cultured neurons, it is also partially inhibited by PD098059, an inhibitor of extracellular signal-regulated protein kinase activation, which indicates an additional contribution of this kinase to high molecular weight microtubule-associated protein 2 phosphorylation at this stage. Both in short-term and long-term cultured neurons, okadaic acid augments high molecular weight microtubule-associated protein 2 phosphorylation at this site through the inhibition of protein phosphatases 1 and/or 2A. Finally, glutamate receptor activation leads to a dephosphorylation of high molecular weight microtubule-associated protein 2 at this site which can also be effectively prevented by okadaic acid. These results are consistent with the participation of glycogen synthase kinase-3, extracellular signal-regulated protein kinases and protein phosphatases 1 and 2A, in the regulation of microtubule-associated protein 2 phosphorylation within living neurons, which may be modulated by extracellular signals like the neurotransmitter glutamate.
|
| pubmed:language |
eng
|
| pubmed:journal | |
| pubmed:citationSubset |
IM
|
| pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Calcium-Calmodulin-Dependent...,
http://linkedlifedata.com/resource/pubmed/chemical/Enzyme Inhibitors,
http://linkedlifedata.com/resource/pubmed/chemical/Flavonoids,
http://linkedlifedata.com/resource/pubmed/chemical/Glycogen Synthase Kinase 3,
http://linkedlifedata.com/resource/pubmed/chemical/Glycogen Synthase Kinases,
http://linkedlifedata.com/resource/pubmed/chemical/Microtubule-Associated Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Mitogen-Activated Protein Kinase 1,
http://linkedlifedata.com/resource/pubmed/chemical/Nerve Tissue Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Okadaic Acid,
http://linkedlifedata.com/resource/pubmed/chemical/PD 98059,
http://linkedlifedata.com/resource/pubmed/chemical/Phosphoprotein Phosphatases,
http://linkedlifedata.com/resource/pubmed/chemical/Phosphothreonine,
http://linkedlifedata.com/resource/pubmed/chemical/Protein Kinases
|
| pubmed:status |
MEDLINE
|
| pubmed:month |
Dec
|
| pubmed:issn |
0306-4522
|
| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:volume |
87
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
861-70
|
| pubmed:dateRevised |
2009-11-19
|
| pubmed:meshHeading |
pubmed-meshheading:9759974-Animals,
pubmed-meshheading:9759974-Calcium-Calmodulin-Dependent Protein Kinases,
pubmed-meshheading:9759974-Cells, Cultured,
pubmed-meshheading:9759974-Cerebellum,
pubmed-meshheading:9759974-Enzyme Inhibitors,
pubmed-meshheading:9759974-Flavonoids,
pubmed-meshheading:9759974-Glycogen Synthase Kinase 3,
pubmed-meshheading:9759974-Glycogen Synthase Kinases,
pubmed-meshheading:9759974-Microtubule-Associated Proteins,
pubmed-meshheading:9759974-Mitogen-Activated Protein Kinase 1,
pubmed-meshheading:9759974-Nerve Tissue Proteins,
pubmed-meshheading:9759974-Neurites,
pubmed-meshheading:9759974-Neurons,
pubmed-meshheading:9759974-Okadaic Acid,
pubmed-meshheading:9759974-Phosphoprotein Phosphatases,
pubmed-meshheading:9759974-Phosphorylation,
pubmed-meshheading:9759974-Phosphothreonine,
pubmed-meshheading:9759974-Protein Kinases,
pubmed-meshheading:9759974-Protein Processing, Post-Translational,
pubmed-meshheading:9759974-Rabbits,
pubmed-meshheading:9759974-Rats,
pubmed-meshheading:9759974-Rats, Wistar
|
| pubmed:year |
1998
|
| pubmed:articleTitle |
Regulation of a site-specific phosphorylation of the microtubule-associated protein 2 during the development of cultured neurons.
|
| pubmed:affiliation |
Centro de Biología Molecular Severo Ochoa, Facultad de Ciencias, Universidad Autónoma de Madrid, Cantoblanco, Spain.
|
| pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
|