Binding of two desmin derivatives to the plasma membrane and the nuclear envelope of avian erythrocytes: evidence for a conserved site-specificity in intermediate filament-membrane interactions
| dc.contributor.author | Georgatos, S. D. | en |
| dc.contributor.author | Weber, K. | en |
| dc.contributor.author | Geisler, N. | en |
| dc.contributor.author | Blobel, G. | en |
| dc.date.accessioned | 2015-11-24T19:32:55Z | |
| dc.date.available | 2015-11-24T19:32:55Z | |
| dc.identifier.issn | 0027-8424 | - |
| dc.identifier.uri | https://olympias.lib.uoi.gr/jspui/handle/123456789/23472 | |
| dc.rights | Default Licence | - |
| dc.subject | Animals | en |
| dc.subject | Binding, Competitive | en |
| dc.subject | Desmin/*blood | en |
| dc.subject | Erythrocyte Membrane/*metabolism | en |
| dc.subject | Erythrocytes/*metabolism | en |
| dc.subject | Kinetics | en |
| dc.subject | Nuclear Envelope/*metabolism | en |
| dc.subject | Protein Binding | en |
| dc.subject | Turkeys | en |
| dc.subject | Vimentin/pharmacology | en |
| dc.title | Binding of two desmin derivatives to the plasma membrane and the nuclear envelope of avian erythrocytes: evidence for a conserved site-specificity in intermediate filament-membrane interactions | en |
| heal.abstract | Using solution binding assays, we found that a 45-kDa fragment of desmin, lacking 67 residues from the N terminus, could specifically associate with avian erythrocyte nuclear envelopes but not with plasma membranes from the same cells. It was also observed that a 50-kDa desmin peptide, missing 27 C-terminal residues, retained the ability to bind to both membrane preparations. Displacement experiments with an excess of purified vimentin suggested that the two desmin derivatives were interacting with a previously identified vimentin receptor at the nuclear envelope, the protein lamin B [Georgatos, S. & Blobel, G. (1987) J. Cell Biol. 105, 117-127]. Additional analysis by affinity chromatography confirmed this conclusion. Employing an overlay assay, we demonstrated that the 50-kDa fragment, but not the 45-kDa desmin peptide, was capable of interacting with the plasma membrane polypeptide ankyrin (a known vimentin attachment site), as was intact vimentin. Conversely, the nuclear envelope protein lamin B was recognized by both fragments but not by a chymotryptic peptide composed solely of the helical rod domain of desmin. These data imply that the lamin B-binding site on desmin resides within the 21 residues following its helical rod domain, whereas the ankyrin-associating region is localized within its N-terminal head domain, exactly as in the case of vimentin. | en |
| heal.access | campus | - |
| heal.fullTextAvailability | TRUE | - |
| heal.identifier.secondary | http://www.ncbi.nlm.nih.gov/pubmed/3477809 | - |
| heal.identifier.secondary | http://www.pnas.org/content/84/19/6780.full.pdf | - |
| heal.journalName | Proc Natl Acad Sci U S A | en |
| heal.journalType | peer-reviewed | - |
| heal.language | en | - |
| heal.publicationDate | 1987 | - |
| 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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