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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
2
|
| pubmed:dateCreated |
1994-11-10
|
| pubmed:abstractText |
We have constructed point mutations in human lamin A cDNA at conserved serine and threonine residues, some of which were shown to be phosphorylated in vitro by cdc2-kinase and protein kinase C and in vivo. Using a functional in vivo assay system, we identified three categories of mutant phenotypes. (i) Dominant negative phenotypes in mitosis result from mutation of Thr-19 and Ser-22 within the amino-terminal cdc2-kinase motif of lamin A. An increase of aberrant mitotic phenotypes in the double mutants Thr-19/Ser-392 and Ser-22/Ser-392 suggests that concomitant phosphorylation of the three residues regulates mitotic lamin A disassembly. (ii) Mutation of both Ser-403/Ser-404 within a PKC motif flanking the nuclear localization signal inhibits transport of mutant lamin A to the nucleus in 64% of the cells. It is proposed that phosphorylation of the motif in vivo positively regulates nuclear localization together with the nuclear localization sequence. (iii) The assembly of lamin A into the perinuclear lamina is disturbed by mutation of the carboxy-terminal Ser-525, previously shown to be interphase-specifically phosphorylated (Eggert et al., Eur. J. Biochem. 213, 659-671 (1993)). The phenotype shows discontinuous and patch-like aggregates of the mutant protein in the nucleus. We suggest that phosphorylation of the site either regulates lamina assembly or lamina-chromatin interaction in interphase.
|
| pubmed:language |
eng
|
| pubmed:journal | |
| pubmed:citationSubset |
IM
|
| pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/DNA,
http://linkedlifedata.com/resource/pubmed/chemical/Lamin Type A,
http://linkedlifedata.com/resource/pubmed/chemical/Lamins,
http://linkedlifedata.com/resource/pubmed/chemical/Nuclear Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Protein Kinase C,
http://linkedlifedata.com/resource/pubmed/chemical/Serine,
http://linkedlifedata.com/resource/pubmed/chemical/Threonine
|
| pubmed:status |
MEDLINE
|
| pubmed:month |
Dec
|
| pubmed:issn |
0171-9335
|
| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:volume |
62
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
237-47
|
| pubmed:dateRevised |
2007-11-15
|
| pubmed:meshHeading |
pubmed-meshheading:7925482-Amino Acid Sequence,
pubmed-meshheading:7925482-Animals,
pubmed-meshheading:7925482-Biological Transport,
pubmed-meshheading:7925482-Cell Line,
pubmed-meshheading:7925482-Cell Nucleus,
pubmed-meshheading:7925482-Chick Embryo,
pubmed-meshheading:7925482-DNA,
pubmed-meshheading:7925482-Fluorescent Antibody Technique,
pubmed-meshheading:7925482-Humans,
pubmed-meshheading:7925482-Lamin Type A,
pubmed-meshheading:7925482-Lamins,
pubmed-meshheading:7925482-Mitosis,
pubmed-meshheading:7925482-Molecular Sequence Data,
pubmed-meshheading:7925482-Mutation,
pubmed-meshheading:7925482-Nuclear Proteins,
pubmed-meshheading:7925482-Phenotype,
pubmed-meshheading:7925482-Phosphorylation,
pubmed-meshheading:7925482-Protein Kinase C,
pubmed-meshheading:7925482-Serine,
pubmed-meshheading:7925482-Threonine,
pubmed-meshheading:7925482-Transfection
|
| pubmed:year |
1993
|
| pubmed:articleTitle |
Functional analysis of phosphorylation sites in human lamin A controlling lamin disassembly, nuclear transport and assembly.
|
| pubmed:affiliation |
Genetisches Institut, Justus-Liebig-Universität, Giessen, Germany.
|
| pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
|