A nuclear envelope-associated kinase phosphorylates arginine-serine motifs and modulates interactions between the lamin B receptor and other nuclear proteins
| dc.contributor.author | Nikolakaki, E. | en |
| dc.contributor.author | Simos, G. | en |
| dc.contributor.author | Georgatos, S. D. | en |
| dc.contributor.author | Giannakouros, T. | en |
| dc.date.accessioned | 2015-11-24T19:40:03Z | |
| dc.date.available | 2015-11-24T19:40:03Z | |
| dc.identifier.issn | 0021-9258 | - |
| dc.identifier.uri | https://olympias.lib.uoi.gr/jspui/handle/123456789/24292 | |
| dc.rights | Default Licence | - |
| dc.subject | Amino Acid Sequence | en |
| dc.subject | Animals | en |
| dc.subject | Arginine/chemistry | en |
| dc.subject | Cell Compartmentation | en |
| dc.subject | Erythrocytes/ultrastructure | en |
| dc.subject | Lamin Type B | en |
| dc.subject | Lamins | en |
| dc.subject | Molecular Sequence Data | en |
| dc.subject | Nuclear Envelope/*enzymology | en |
| dc.subject | Nuclear Proteins/metabolism | en |
| dc.subject | Peptides/chemistry/metabolism | en |
| dc.subject | Phosphoserine/metabolism | en |
| dc.subject | Protein-Serine-Threonine Kinases/*metabolism | en |
| dc.subject | Receptors, Cytoplasmic and Nuclear/*metabolism | en |
| dc.subject | Structure-Activity Relationship | en |
| dc.subject | Substrate Specificity | en |
| dc.subject | Turkeys | en |
| dc.title | A nuclear envelope-associated kinase phosphorylates arginine-serine motifs and modulates interactions between the lamin B receptor and other nuclear proteins | en |
| heal.abstract | Previous studies have identified a subassembly of nuclear envelope proteins, termed "the LBR complex." This complex includes the lamin B receptor protein (LBR or p58), a kinase which phosphorylates LBR in a constitutive fashion (LBR kinase), the nuclear lamins A and B, an 18-kDa polypeptide (p18), and a 34-kDa protein (p34/p32). The latter polypeptide has been shown to interact with the HIV-1 proteins Rev and Tat and with the splicing factor 2 (SF2). Using recombinant proteins produced in bacteria and synthetic peptides representing different regions of LBR, we now show that the LBR kinase modifies specifically arginine-serine (RS) dipeptide motifs located at the nucleoplasmic, NH2-terminal domain of LBR and in members of the SR family of splicing factors. Furthermore, we show that the NH2-terminal domain of LBR binds to p34/p32, whereas a mutated domain lacking the RS region does not. Phosphorylation of LBR by the RS kinase completely abolishes binding of p34/p32, suggesting that this enzyme regulates interactions among the components of the LBR complex. | en |
| heal.access | campus | - |
| heal.fullTextAvailability | TRUE | - |
| heal.identifier.secondary | http://www.ncbi.nlm.nih.gov/pubmed/8626534 | - |
| heal.identifier.secondary | http://www.jbc.org/content/271/14/8365.full.pdf | - |
| heal.journalName | J Biol Chem | en |
| heal.journalType | peer-reviewed | - |
| heal.language | en | - |
| heal.publicationDate | 1996 | - |
| 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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