Publication

Anchoring of protein kinase A-regulatory subunit II alpha to subapically positioned centrosomes mediates apical bile canalicular lumen development in response to oncostatin m but not cAMP

Wojtal, K. A., Hoekstra, D. & van Ijzendoorn, S. C. D., Jul-2007, In : Molecular Biology of the Cell. 18, 7, p. 2745-2754 10 p.

Research output: Contribution to journalArticleAcademicpeer-review

APA

Wojtal, K. A., Hoekstra, D., & van Ijzendoorn, S. C. D. (2007). Anchoring of protein kinase A-regulatory subunit II alpha to subapically positioned centrosomes mediates apical bile canalicular lumen development in response to oncostatin m but not cAMP. Molecular Biology of the Cell, 18(7), 2745-2754. https://doi.org/10.1091/mbc.E06-08-0732

Author

Wojtal, Kacper A. ; Hoekstra, Dick ; van Ijzendoorn, Sven C. D. / Anchoring of protein kinase A-regulatory subunit II alpha to subapically positioned centrosomes mediates apical bile canalicular lumen development in response to oncostatin m but not cAMP. In: Molecular Biology of the Cell. 2007 ; Vol. 18, No. 7. pp. 2745-2754.

Harvard

Wojtal, KA, Hoekstra, D & van Ijzendoorn, SCD 2007, 'Anchoring of protein kinase A-regulatory subunit II alpha to subapically positioned centrosomes mediates apical bile canalicular lumen development in response to oncostatin m but not cAMP', Molecular Biology of the Cell, vol. 18, no. 7, pp. 2745-2754. https://doi.org/10.1091/mbc.E06-08-0732

Standard

Anchoring of protein kinase A-regulatory subunit II alpha to subapically positioned centrosomes mediates apical bile canalicular lumen development in response to oncostatin m but not cAMP. / Wojtal, Kacper A.; Hoekstra, Dick; van Ijzendoorn, Sven C. D.

In: Molecular Biology of the Cell, Vol. 18, No. 7, 07.2007, p. 2745-2754.

Research output: Contribution to journalArticleAcademicpeer-review

Vancouver

Wojtal KA, Hoekstra D, van Ijzendoorn SCD. Anchoring of protein kinase A-regulatory subunit II alpha to subapically positioned centrosomes mediates apical bile canalicular lumen development in response to oncostatin m but not cAMP. Molecular Biology of the Cell. 2007 Jul;18(7):2745-2754. https://doi.org/10.1091/mbc.E06-08-0732


BibTeX

@article{05ba896bc5e8482ea0e659c5e0a142d2,
title = "Anchoring of protein kinase A-regulatory subunit II alpha to subapically positioned centrosomes mediates apical bile canalicular lumen development in response to oncostatin m but not cAMP",
abstract = "Oncostatin M and cAMP signaling stimulate apical surface-directed membrane trafficking and apical lumen development in hepatocytes, both in a protein kinase A (PKA)-dependent manner. Here, we show that oncostatin M, but not cAMP, promotes the A-kinase anchoring protein (AKAP)-dependent anchoring of the PKA regulatory subunit (R)II alpha to subapical centrosomes and that this requires extracellular signal-regulated kinase 2 activation. Stable expression of the RII-displacing peptide AKAP-IS, but not a scrambled peptide, inhibits the association of RII alpha with centrosomal AKAPs and results in the repositioning of the centrosome from a subapical to a perinuclear location. Concomitantly, common endosomes, but not apical recycling endosomes, are repositioned from a subapical to a perinuclear location, without significant effects on constitutive or oncostatin M-stimulated basolateral-to-apical transcytosis. Importantly, however, the expression of the AKAP-IS peptide completely blocks oncostatin M-, but not cAMP-stimulated apical lumen development. Together, the data suggest that centrosomal anchoring of RII alpha and the interrelated subapical positioning of these centrosomes is required for oncostatin M-, but not cAMP-mediated, bile canalicular lumen development in a manner that is uncoupled from oncostatin M-stimulated apical lumen-directed membrane trafficking. The results also imply that multiple PKA-mediated signaling pathways control apical lumen development and that subapical centrosome positioning is important in some of these pathways.",
keywords = "CANINE KIDNEY-CELLS, POLARIZED SPHINGOLIPID TRANSPORT, RAT HEPATOCYTE COUPLETS, HEPG2 CELLS, EPITHELIAL-CELLS, MICROTUBULE ORGANIZATION, MEMBRANE BIOGENESIS, SIGNAL-TRANSDUCTION, RECYCLING SYSTEM, MDCK CELLS",
author = "Wojtal, {Kacper A.} and Dick Hoekstra and {van Ijzendoorn}, {Sven C. D.}",
year = "2007",
month = "7",
doi = "10.1091/mbc.E06-08-0732",
language = "English",
volume = "18",
pages = "2745--2754",
journal = "Molecular Biology of the Cell",
issn = "1059-1524",
publisher = "AMER SOC CELL BIOLOGY",
number = "7",

}

RIS

TY - JOUR

T1 - Anchoring of protein kinase A-regulatory subunit II alpha to subapically positioned centrosomes mediates apical bile canalicular lumen development in response to oncostatin m but not cAMP

AU - Wojtal, Kacper A.

AU - Hoekstra, Dick

AU - van Ijzendoorn, Sven C. D.

PY - 2007/7

Y1 - 2007/7

N2 - Oncostatin M and cAMP signaling stimulate apical surface-directed membrane trafficking and apical lumen development in hepatocytes, both in a protein kinase A (PKA)-dependent manner. Here, we show that oncostatin M, but not cAMP, promotes the A-kinase anchoring protein (AKAP)-dependent anchoring of the PKA regulatory subunit (R)II alpha to subapical centrosomes and that this requires extracellular signal-regulated kinase 2 activation. Stable expression of the RII-displacing peptide AKAP-IS, but not a scrambled peptide, inhibits the association of RII alpha with centrosomal AKAPs and results in the repositioning of the centrosome from a subapical to a perinuclear location. Concomitantly, common endosomes, but not apical recycling endosomes, are repositioned from a subapical to a perinuclear location, without significant effects on constitutive or oncostatin M-stimulated basolateral-to-apical transcytosis. Importantly, however, the expression of the AKAP-IS peptide completely blocks oncostatin M-, but not cAMP-stimulated apical lumen development. Together, the data suggest that centrosomal anchoring of RII alpha and the interrelated subapical positioning of these centrosomes is required for oncostatin M-, but not cAMP-mediated, bile canalicular lumen development in a manner that is uncoupled from oncostatin M-stimulated apical lumen-directed membrane trafficking. The results also imply that multiple PKA-mediated signaling pathways control apical lumen development and that subapical centrosome positioning is important in some of these pathways.

AB - Oncostatin M and cAMP signaling stimulate apical surface-directed membrane trafficking and apical lumen development in hepatocytes, both in a protein kinase A (PKA)-dependent manner. Here, we show that oncostatin M, but not cAMP, promotes the A-kinase anchoring protein (AKAP)-dependent anchoring of the PKA regulatory subunit (R)II alpha to subapical centrosomes and that this requires extracellular signal-regulated kinase 2 activation. Stable expression of the RII-displacing peptide AKAP-IS, but not a scrambled peptide, inhibits the association of RII alpha with centrosomal AKAPs and results in the repositioning of the centrosome from a subapical to a perinuclear location. Concomitantly, common endosomes, but not apical recycling endosomes, are repositioned from a subapical to a perinuclear location, without significant effects on constitutive or oncostatin M-stimulated basolateral-to-apical transcytosis. Importantly, however, the expression of the AKAP-IS peptide completely blocks oncostatin M-, but not cAMP-stimulated apical lumen development. Together, the data suggest that centrosomal anchoring of RII alpha and the interrelated subapical positioning of these centrosomes is required for oncostatin M-, but not cAMP-mediated, bile canalicular lumen development in a manner that is uncoupled from oncostatin M-stimulated apical lumen-directed membrane trafficking. The results also imply that multiple PKA-mediated signaling pathways control apical lumen development and that subapical centrosome positioning is important in some of these pathways.

KW - CANINE KIDNEY-CELLS

KW - POLARIZED SPHINGOLIPID TRANSPORT

KW - RAT HEPATOCYTE COUPLETS

KW - HEPG2 CELLS

KW - EPITHELIAL-CELLS

KW - MICROTUBULE ORGANIZATION

KW - MEMBRANE BIOGENESIS

KW - SIGNAL-TRANSDUCTION

KW - RECYCLING SYSTEM

KW - MDCK CELLS

U2 - 10.1091/mbc.E06-08-0732

DO - 10.1091/mbc.E06-08-0732

M3 - Article

VL - 18

SP - 2745

EP - 2754

JO - Molecular Biology of the Cell

JF - Molecular Biology of the Cell

SN - 1059-1524

IS - 7

ER -

ID: 4579925