rdf:type |
|
lifeskim:mentions |
|
pubmed:issue |
2
|
pubmed:dateCreated |
1991-8-22
|
pubmed:abstractText |
Effects of phosphorylation of the neurofilament L protein (NF-L) on the reassembly system were studied by both sedimentation experiments and low-angle rotary shadowing. Bovine spinal cord NF-L was phosphorylated with 3-4 mol/mol protein by either the catalytic subunit of cAMP-dependent protein kinase or protein kinase C. Phosphorylated NF-L could not assemble into filaments. Phosphorylation by either cAMP-dependent protein kinase or protein kinase C inhibited the same step of the reassembly process. Phosphorylated NF-L remained as an 8-chain complex even in favorable conditions for reassembly. The extent of the effect of phosphorylation on the filamentous structure of NF-L was also investigated by using the catalytic subunit of cAMP-dependent protein kinase. The amount of unassembled NF-L increased linearly with increased phosphorylation in the sedimentation experiments. Structural observations indicated that 1 or 2 mol of phosphorylation is enough to inhibit reassembly and to induce disassembly, and the disassembly process was also observed. The filaments were shown to unravel with disassembly. Star-like clusters, which we reported as being the initial stage of reassembly, were also identified.
|
pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/2100199-2417512,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2100199-2418034,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2100199-2465294,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2100199-2491851,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2100199-2494168,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2100199-2500966,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2100199-2536033,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2100199-2538587,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2100199-2648386,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2100199-2833525,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2100199-2839368,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2100199-2844152,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2100199-2925792,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2100199-2926480,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2100199-2982842,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2100199-3039376,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2100199-3052284,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2100199-3172218,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2100199-3359992,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2100199-3722268,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2100199-3782120,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2100199-3903168,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2100199-3920075,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2100199-3926771,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2100199-4039683,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2100199-4375763,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2100199-5432063,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2100199-6155474,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2100199-6176713,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2100199-6181077,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2100199-6182147,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2100199-6195164,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2100199-6204990,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2100199-6286144,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2100199-6313713,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2100199-6425303,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2100199-6802980,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2100199-7188712,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2100199-7202005,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2100199-7202006
|
pubmed:language |
eng
|
pubmed:journal |
|
pubmed:citationSubset |
IM
|
pubmed:chemical |
|
pubmed:status |
MEDLINE
|
pubmed:month |
Jan
|
pubmed:issn |
1044-2030
|
pubmed:author |
|
pubmed:issnType |
Print
|
pubmed:volume |
1
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
237-48
|
pubmed:dateRevised |
2009-11-19
|
pubmed:meshHeading |
|
pubmed:year |
1990
|
pubmed:articleTitle |
Effects of phosphorylation of the neurofilament L protein on filamentous structures.
|
pubmed:affiliation |
Department of Anatomy and Cell Biology, Faculty of Medicine, University of Tokyo, Japan.
|
pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
|