dc.contributor.author |
Lou, H |
en |
dc.contributor.author |
Smith, AM |
en |
dc.contributor.author |
Coates, LC |
en |
dc.contributor.author |
Cawley, NX |
en |
dc.contributor.author |
Loh, YP |
en |
dc.contributor.author |
Birch, Nigel |
en |
dc.date.accessioned |
2012-03-01T01:20:14Z |
en |
dc.date.issued |
2007-03-15 |
en |
dc.identifier.citation |
Molecular and Cellular Endocrinology 267(1-2):17-25 15 Mar 2007 |
en |
dc.identifier.issn |
0303-7207 |
en |
dc.identifier.uri |
http://hdl.handle.net/2292/12393 |
en |
dc.description.abstract |
The biosynthesis of hormones and neuropeptides involves post-translational cleavage of precursors at basic amino acids by prohormone convertases (PCs) predominantly in secretory granules that bud from the trans-Golgi Network. This study reports that the amino acid sequence of PC3 (aa617–638), previously identified as a novel transmembrane (TM) domain, confers lipid raft association and facilitates sorting of the enzyme to the secretory granules of Neuro2A cells for prohormone cleavage. Floatation analysis on sucrose density gradients showed that a proportion of full length (PC3-FL) and carboxyl terminus-truncated PC31–638 (PC3-638) containing the TM domain were associated with lipid rafts in Neuro2A cells, while PC31–616 (PC3-616) and PC3-ΔTM lacking the TM domain were not. Secondly, PC3-FL and PC3-638 underwent stimulated secretion and were shown to be colocalized with a secretory granule marker, chromogranin A, by immunocytochemistry. In contrast, PC3-616 and PC3-ΔTM were constitutively secreted and primarily localized in the Golgi. These data indicate that the transmembrane domain of PC3 plays a key role in sorting the enzyme to the regulated secretory pathway. |
en |
dc.language |
EN |
en |
dc.publisher |
ELSEVIER IRELAND LTD |
en |
dc.relation.ispartofseries |
Molecular and Cellular Endocrinology |
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/0303-7207/ |
en |
dc.rights.uri |
https://researchspace.auckland.ac.nz/docs/uoa-docs/rights.htm |
en |
dc.subject |
prohormone convertase |
en |
dc.subject |
enzyme |
en |
dc.subject |
sorting |
en |
dc.subject |
lipid raft |
en |
dc.subject |
transmembrane protein |
en |
dc.subject |
CARBOXYPEPTIDASE-E |
en |
dc.subject |
SORTING RECEPTOR |
en |
dc.subject |
MEMBRANE-ASSOCIATION |
en |
dc.subject |
CELLULAR TRAFFICKING |
en |
dc.subject |
LIPID RAFTS |
en |
dc.subject |
PROTEINS |
en |
dc.subject |
SEQUENCE |
en |
dc.subject |
GRANULES |
en |
dc.subject |
FURIN |
en |
dc.subject |
SPC3 |
en |
dc.title |
The transmembrane domain of the prohormone convertase PC3: A key motif for targeting to the regulated secretory pathway |
en |
dc.type |
Journal Article |
en |
dc.identifier.doi |
10.1016/j.mce.2006.11.011 |
en |
pubs.issue |
1-2 |
en |
pubs.begin-page |
17 |
en |
pubs.volume |
267 |
en |
dc.rights.holder |
Copyright: Elsevier Ireland Ltd. |
en |
dc.identifier.pmid |
17240044 |
en |
pubs.end-page |
25 |
en |
dc.rights.accessrights |
http://purl.org/eprint/accessRights/RestrictedAccess |
en |
pubs.subtype |
Article |
en |
pubs.elements-id |
113318 |
en |
pubs.record-created-at-source-date |
2012-02-21 |
en |
pubs.dimensions-id |
17240044 |
en |