dc.contributor.author |
Bai, Jizhong |
en |
dc.contributor.author |
Leung, Yee Fun |
en |
dc.contributor.author |
Holloway, Hilary |
en |
dc.contributor.author |
Krissansen, Geoffrey |
en |
dc.date.accessioned |
2012-03-15T22:07:22Z |
en |
dc.date.issued |
2008 |
en |
dc.identifier.citation |
CELL BIOLOGY INTERNATIONAL 32(5):473-483 01 May 2008 |
en |
dc.identifier.issn |
1065-6995 |
en |
dc.identifier.uri |
http://hdl.handle.net/2292/14476 |
en |
dc.description.abstract |
Expression of the canine 180-kDa ribosome receptor p180 in yeast induces the synthesis of RER, and increases the mRNAs of secretory pathway proteins, and protein secretion. To assess whether p180 is a master regulator of cell secretion in mammalian cells, we stably expressed red fluorescent forms of the human p180 variants p180ΔR (no tandem repeats), p180R (26 repeats), and full-length p180FR (54 repeats) containing different lengths of the tandem repeat ribosome-binding domain in rat pancreatic RINm5F islet β-cells. All three fluorescent p180 variants localized exclusively to the RER. Cells transfected with p180R were filled with ribosome-studded karmellae, whereas p180ΔR and p180FR transfectants contained only increased amounts of mostly smooth ER. Unlike in yeast, over-expression of p180R failed to increase the secretory pathway proteins calnexin, SEC61β, and calreticulin, or ribosome biogenesis. The data suggest that alternative splicing of the p180 tandem repeat domain is a means of regulating the ribosome-binding activity of p180, and potentially the secretory activity of the cell. However, p180 is not a master regulator of mammalian cell secretion as it does not concomitantly trigger the synthesis of protein machinery required to enhance protein synthesis and cell secretion. |
en |
dc.publisher |
Portland Press Limited |
en |
dc.relation.ispartofseries |
Cell Biology International |
en |
dc.rights |
Items in ResearchSpace are protected by copyright, with all rights reserved, unless otherwise indicated. Previously published items are made available in accordance with the copyright policy of the publisher.
Details obtained from http://www.sherpa.ac.uk/romeo/issn/1065-6995/ |
en |
dc.rights.uri |
https://researchspace.auckland.ac.nz/docs/uoa-docs/rights.htm |
en |
dc.title |
Alternatively spliced forms of the P180 ribosome receptor differ in their ability to induce the proliferation of rough endoplasmic reticulum |
en |
dc.type |
Journal Article |
en |
dc.identifier.doi |
10.1016/j.cellbi.2007.10.002 |
en |
pubs.issue |
5 |
en |
pubs.begin-page |
473 |
en |
pubs.volume |
32 |
en |
dc.rights.holder |
Copyright: Portland Press Limited |
en |
dc.identifier.pmid |
18083570 |
en |
pubs.end-page |
483 |
en |
dc.rights.accessrights |
http://purl.org/eprint/accessRights/RestrictedAccess |
en |
pubs.subtype |
Article |
en |
pubs.elements-id |
80055 |
en |
pubs.org-id |
Medical and Health Sciences |
en |
pubs.org-id |
Medical Sciences |
en |
pubs.org-id |
Auckland Cancer Research |
en |
pubs.org-id |
Physiology Division |
en |
dc.identifier.eissn |
1095-8355 |
en |
pubs.record-created-at-source-date |
2010-09-01 |
en |
pubs.dimensions-id |
18083570 |
en |