Heterotypic and homotypic associations between the nuclear lamins: site-specificity and control by phosphorylation
| dc.contributor.author | Georgatos, S. D. | en |
| dc.contributor.author | Stournaras, C. | en |
| dc.contributor.author | Blobel, G. | en |
| dc.date.accessioned | 2015-11-24T19:13:55Z | |
| dc.date.available | 2015-11-24T19:13:55Z | |
| dc.identifier.issn | 0027-8424 | - |
| dc.identifier.uri | https://olympias.lib.uoi.gr/jspui/handle/123456789/21240 | |
| dc.rights | Default Licence | - |
| dc.subject | Adenosine Triphosphate/metabolism | en |
| dc.subject | Animals | en |
| dc.subject | Cell Nucleus/metabolism | en |
| dc.subject | Iodine Radioisotopes | en |
| dc.subject | Lamin Type A | en |
| dc.subject | Lamin Type B | en |
| dc.subject | Lamins | en |
| dc.subject | Liver/metabolism | en |
| dc.subject | Macromolecular Substances | en |
| dc.subject | Nuclear Proteins/isolation & purification/*metabolism | en |
| dc.subject | Phosphorus Radioisotopes | en |
| dc.subject | Phosphorylation | en |
| dc.subject | Rats | en |
| dc.title | Heterotypic and homotypic associations between the nuclear lamins: site-specificity and control by phosphorylation | en |
| heal.abstract | Using purified components in affinity chromatography and blot binding assays, we have found that rat liver lamins A, B, and C can associate in homotypic and heterotypic fashions. Heterotypic A-B and C-B complexes are unusually stable and involve the common amino-terminal domain of lamins A and C, but not their helical "rod" domain. A synthetic peptide, comprising the first 32 amino acid residues of lamins A and C, is able to fully compete with the intact molecules for binding to lamin B. Conversely, heterotypic A-C associations and homotypic A-A and C-C interactions appear significantly weaker than A/C-B binding and do not involve the lamin A and C amino-terminal domain. Homotypic B-B complexes are not formed to any considerable extent unless isolated lamin B subunits are "superphosphorylated" in vitro with protein kinase A. However, when lamins A and C are similarly modified, no changes in their binding specificity can be detected. These data suggest that the nuclear lamina, unlike other multicomponent intermediate filaments, constitutes a nonobligatory heteropolymer. They also indicate that cAMP-dependent phosphorylation of interphase lamin B could cause remodeling of the lamina and establishment of homopolymeric domains. | en |
| heal.access | campus | - |
| heal.fullTextAvailability | TRUE | - |
| heal.identifier.secondary | http://www.ncbi.nlm.nih.gov/pubmed/3380795 | - |
| heal.identifier.secondary | http://www.pnas.org/content/85/12/4325.full.pdf | - |
| heal.journalName | Proc Natl Acad Sci U S A | en |
| heal.journalType | peer-reviewed | - |
| heal.language | en | - |
| heal.publicationDate | 1988 | - |
| heal.recordProvider | Πανεπιστήμιο Ιωαννίνων. Σχολή Επιστημών Υγείας. Τμήμα Ιατρικής | el |
| heal.type | journalArticle | - |
| heal.type.el | Άρθρο Περιοδικού | el |
| heal.type.en | Journal article | en |
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