Disparate effects of p24alpha and p24delta on secretory protein transport and processing.
BACKGROUND: The p24 family is thought to be somehow involved in endoplasmic reticulum (ER)-to-Golgi protein transport. A subset of the p24 proteins (p24alpha(3), -beta(1), -gamma(3) and -delta(2)) is upregulated when Xenopus laevis intermediate pituitary melanotrope cells are physiologically activat...
Main Authors: | , , , |
---|---|
Format: | Article |
Language: | English |
Published: |
Public Library of Science (PLoS)
2007-01-01
|
Series: | PLoS ONE |
Online Access: | http://europepmc.org/articles/PMC1933603?pdf=render |
_version_ | 1818024548076879872 |
---|---|
author | Jeroen R P M Strating Gerrit Bouw Theo G M Hafmans Gerard J M Martens |
author_facet | Jeroen R P M Strating Gerrit Bouw Theo G M Hafmans Gerard J M Martens |
author_sort | Jeroen R P M Strating |
collection | DOAJ |
description | BACKGROUND: The p24 family is thought to be somehow involved in endoplasmic reticulum (ER)-to-Golgi protein transport. A subset of the p24 proteins (p24alpha(3), -beta(1), -gamma(3) and -delta(2)) is upregulated when Xenopus laevis intermediate pituitary melanotrope cells are physiologically activated to produce vast amounts of their major secretory cargo, the prohormone proopiomelanocortin (POMC). METHODOLOGY/PRINCIPAL FINDINGS: Here we find that transgene expression of p24alpha(3 )or p24delta(2) specifically in the Xenopus melanotrope cells in both cases causes an effective displacement of the endogenous p24 proteins, resulting in severely distorted p24 systems and disparate melanotrope cell phenotypes. Transgene expression of p24alpha(3) greatly reduces POMC transport and leads to accumulation of the prohormone in large, ER-localized electron-dense structures, whereas p24delta(2)-transgenesis does not influence the overall ultrastructure of the cells nor POMC transport and cleavage, but affects the Golgi-based processes of POMC glycomaturation and sulfation. CONCLUSIONS/SIGNIFICANCE: Transgenic expression of two distinct p24 family members has disparate effects on secretory pathway functioning, illustrating the specificity and non-redundancy of our transgenic approach. We conclude that members of the p24 family furnish subcompartments of the secretory pathway with specific sets of machinery cargo to provide the proper microenvironments for efficient and correct secretory protein transport and processing. |
first_indexed | 2024-12-10T04:01:58Z |
format | Article |
id | doaj.art-13f582413b154ca6954fa956cdcd9fdb |
institution | Directory Open Access Journal |
issn | 1932-6203 |
language | English |
last_indexed | 2024-12-10T04:01:58Z |
publishDate | 2007-01-01 |
publisher | Public Library of Science (PLoS) |
record_format | Article |
series | PLoS ONE |
spelling | doaj.art-13f582413b154ca6954fa956cdcd9fdb2022-12-22T02:02:57ZengPublic Library of Science (PLoS)PLoS ONE1932-62032007-01-0128e70410.1371/journal.pone.0000704Disparate effects of p24alpha and p24delta on secretory protein transport and processing.Jeroen R P M StratingGerrit BouwTheo G M HafmansGerard J M MartensBACKGROUND: The p24 family is thought to be somehow involved in endoplasmic reticulum (ER)-to-Golgi protein transport. A subset of the p24 proteins (p24alpha(3), -beta(1), -gamma(3) and -delta(2)) is upregulated when Xenopus laevis intermediate pituitary melanotrope cells are physiologically activated to produce vast amounts of their major secretory cargo, the prohormone proopiomelanocortin (POMC). METHODOLOGY/PRINCIPAL FINDINGS: Here we find that transgene expression of p24alpha(3 )or p24delta(2) specifically in the Xenopus melanotrope cells in both cases causes an effective displacement of the endogenous p24 proteins, resulting in severely distorted p24 systems and disparate melanotrope cell phenotypes. Transgene expression of p24alpha(3) greatly reduces POMC transport and leads to accumulation of the prohormone in large, ER-localized electron-dense structures, whereas p24delta(2)-transgenesis does not influence the overall ultrastructure of the cells nor POMC transport and cleavage, but affects the Golgi-based processes of POMC glycomaturation and sulfation. CONCLUSIONS/SIGNIFICANCE: Transgenic expression of two distinct p24 family members has disparate effects on secretory pathway functioning, illustrating the specificity and non-redundancy of our transgenic approach. We conclude that members of the p24 family furnish subcompartments of the secretory pathway with specific sets of machinery cargo to provide the proper microenvironments for efficient and correct secretory protein transport and processing.http://europepmc.org/articles/PMC1933603?pdf=render |
spellingShingle | Jeroen R P M Strating Gerrit Bouw Theo G M Hafmans Gerard J M Martens Disparate effects of p24alpha and p24delta on secretory protein transport and processing. PLoS ONE |
title | Disparate effects of p24alpha and p24delta on secretory protein transport and processing. |
title_full | Disparate effects of p24alpha and p24delta on secretory protein transport and processing. |
title_fullStr | Disparate effects of p24alpha and p24delta on secretory protein transport and processing. |
title_full_unstemmed | Disparate effects of p24alpha and p24delta on secretory protein transport and processing. |
title_short | Disparate effects of p24alpha and p24delta on secretory protein transport and processing. |
title_sort | disparate effects of p24alpha and p24delta on secretory protein transport and processing |
url | http://europepmc.org/articles/PMC1933603?pdf=render |
work_keys_str_mv | AT jeroenrpmstrating disparateeffectsofp24alphaandp24deltaonsecretoryproteintransportandprocessing AT gerritbouw disparateeffectsofp24alphaandp24deltaonsecretoryproteintransportandprocessing AT theogmhafmans disparateeffectsofp24alphaandp24deltaonsecretoryproteintransportandprocessing AT gerardjmmartens disparateeffectsofp24alphaandp24deltaonsecretoryproteintransportandprocessing |