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https://olympias.lib.uoi.gr/jspui/handle/123456789/15823Full metadata record
| DC Field | Value | Language |
|---|---|---|
| dc.contributor.author | Papanikolaou, A. | en |
| dc.contributor.author | Papafotika, A. | en |
| dc.contributor.author | Christoforidis, S. | en |
| dc.date.accessioned | 2015-11-24T17:58:03Z | - |
| dc.date.available | 2015-11-24T17:58:03Z | - |
| dc.identifier.issn | 1398-9219 | - |
| dc.identifier.uri | https://olympias.lib.uoi.gr/jspui/handle/123456789/15823 | - |
| dc.rights | Default Licence | - |
| dc.subject | apical transport | en |
| dc.subject | biosynthetic transport | en |
| dc.subject | cd39/ntpdase1 | en |
| dc.subject | n-glycosylation | en |
| dc.subject | polarized transport | en |
| dc.subject | protein processing | en |
| dc.subject | protein sorting | en |
| dc.subject | protein trafficking | en |
| dc.subject | transmembrane domains | en |
| dc.subject | nucleoside triphosphate diphosphohydrolase-1 | en |
| dc.subject | influenza-virus hemagglutinin | en |
| dc.subject | polarized mdck cells | en |
| dc.subject | trans-golgi network | en |
| dc.subject | canine kidney-cells | en |
| dc.subject | placental atp-diphosphohydrolase | en |
| dc.subject | linked oligosaccharides affect | en |
| dc.subject | ecto-nucleotidase cd39 | en |
| dc.subject | xaa-thr sequons | en |
| dc.subject | n-glycosylation | en |
| dc.title | CD39 Reveals Novel Insights into the Role of Transmembrane Domains in Protein Processing, Apical Targeting and Activity | en |
| heal.type | journalArticle | - |
| heal.type.en | Journal article | en |
| heal.type.el | Άρθρο Περιοδικού | el |
| heal.identifier.secondary | <Go to ISI>://000293797200006 | - |
| heal.identifier.secondary | http://onlinelibrary.wiley.com/store/10.1111/j.1600-0854.2011.01224.x/asset/j.1600-0854.2011.01224.x.pdf?v=1&t=h0xqmk7d&s=8d68602d747a00c6a3d8298ac6381861b3d5bb10 | - |
| heal.language | en | - |
| heal.access | campus | - |
| heal.recordProvider | Πανεπιστήμιο Ιωαννίνων. Σχολή Επιστημών και Τεχνολογιών. Τμήμα Βιολογικών Εφαρμογών και Τεχνολογιών | el |
| heal.publicationDate | 2011 | - |
| heal.abstract | Cargo proteins of the biosynthetic secretory pathway are folded in the endoplasmic reticulum (ER) and proceed to the trans Golgi network for sorting and targeting to the apical or basolateral sides of the membrane, where they exert their function. These processes depend on diverse protein domains. Here, we used CD39 (NTPdase1), a modulator of thrombosis and inflammation, which contains an extracellular and two transmembrane domains (TMDs), as a model protein to address comprehensively the role of native TMDs in folding, polarized transport and biological activity. In MDCK cells, CD39 exits Golgi dynamin-dependently and is targeted to the apical side of themembrane. Although the N-terminal TMD possesses an apical targeting signal, the N- and C-terminal TMDs are not required for apical targeting of CD39. Folding and transport to the plasma membrane relies only on the C-terminal TMD, while the N- terminal one is redundant. Nevertheless, both N- and C-terminal anchoring as well as genuine TMDs are critical for optimal enzymatic activity and activation by cholesterol. We conclude therefore that TMDs are not just mechanical linkers between proteins and membranes but are also able to control folding and sorting, as well as biological activity via sensing components of lipid bilayers. | en |
| heal.journalName | Traffic | en |
| heal.journalType | peer reviewed | - |
| heal.fullTextAvailability | TRUE | - |
| Appears in Collections: | Άρθρα σε επιστημονικά περιοδικά ( Ανοικτά) | |
Files in This Item:
| File | Description | Size | Format | |
|---|---|---|---|---|
| Papanikolaou-2011-CD39 Reveals Novel I.pdf | 5.47 MB | Adobe PDF | View/Open Request a copy |
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