Publication

The Na+/H+ Exchanger NHE6 in the Endosomal Recycling System Is Involved in the Development of Apical Bile Canalicular Surface Domains in HepG2 Cells

Ohgaki, R., Matsushita, M., Kanazawa, H., Ogihara, S., Hoekstra, D. & van IJzendoorn, S. C. D., 1-Apr-2010, In : Molecular Biology of the Cell. 21, 7, p. 1293-1304 12 p.

Research output: Contribution to journalArticleAcademicpeer-review

APA

Ohgaki, R., Matsushita, M., Kanazawa, H., Ogihara, S., Hoekstra, D., & van IJzendoorn, S. C. D. (2010). The Na+/H+ Exchanger NHE6 in the Endosomal Recycling System Is Involved in the Development of Apical Bile Canalicular Surface Domains in HepG2 Cells. Molecular Biology of the Cell, 21(7), 1293-1304. https://doi.org/10.1091/mbc.E09-09-0767

Author

Ohgaki, Ryuichi ; Matsushita, Masafumi ; Kanazawa, Hiroshi ; Ogihara, Satoshi ; Hoekstra, Dick ; van IJzendoorn, Sven C. D. / The Na+/H+ Exchanger NHE6 in the Endosomal Recycling System Is Involved in the Development of Apical Bile Canalicular Surface Domains in HepG2 Cells. In: Molecular Biology of the Cell. 2010 ; Vol. 21, No. 7. pp. 1293-1304.

Harvard

Ohgaki, R, Matsushita, M, Kanazawa, H, Ogihara, S, Hoekstra, D & van IJzendoorn, SCD 2010, 'The Na+/H+ Exchanger NHE6 in the Endosomal Recycling System Is Involved in the Development of Apical Bile Canalicular Surface Domains in HepG2 Cells', Molecular Biology of the Cell, vol. 21, no. 7, pp. 1293-1304. https://doi.org/10.1091/mbc.E09-09-0767

Standard

The Na+/H+ Exchanger NHE6 in the Endosomal Recycling System Is Involved in the Development of Apical Bile Canalicular Surface Domains in HepG2 Cells. / Ohgaki, Ryuichi; Matsushita, Masafumi; Kanazawa, Hiroshi; Ogihara, Satoshi; Hoekstra, Dick; van IJzendoorn, Sven C. D.

In: Molecular Biology of the Cell, Vol. 21, No. 7, 01.04.2010, p. 1293-1304.

Research output: Contribution to journalArticleAcademicpeer-review

Vancouver

Ohgaki R, Matsushita M, Kanazawa H, Ogihara S, Hoekstra D, van IJzendoorn SCD. The Na+/H+ Exchanger NHE6 in the Endosomal Recycling System Is Involved in the Development of Apical Bile Canalicular Surface Domains in HepG2 Cells. Molecular Biology of the Cell. 2010 Apr 1;21(7):1293-1304. https://doi.org/10.1091/mbc.E09-09-0767


BibTeX

@article{467066bc40f64994876176b0de4aea32,
title = "The Na+/H+ Exchanger NHE6 in the Endosomal Recycling System Is Involved in the Development of Apical Bile Canalicular Surface Domains in HepG2 Cells",
abstract = "Polarized epithelial cells develop and maintain distinct apical and basolateral surface domains despite a continuous flux of membranes between these domains. The Na+/H+ exchanger NHE6 localizes to endosomes but its function is unknown. Here, we demonstrate that polarized hepatoma HepG2 cells express an NHE6.1 variant that localizes to recycling endosomes and colocalizes with transcytosing bulk membrane lipids. NHE6.1 knockdown or overexpression decreases or increases recycling endosome pH, respectively, and inhibits the maintenance of apical, bile canalicular plasma membranes and, concomitantly, apical lumens. NHE6.1 knockdown or overexpression has little effect on the de novo biogenesis of apical surface domains. NHE6.1 knockdown does not inhibit basolateral-to-apical transcytosis of bulk membrane lipids, but it does promote their progressive loss from the apical surface, leaving cells unable to efficiently retain bulk membrane and bile canalicular proteins at the apical surface. The data suggest that a limited range of endosome pH mediated by NHE6.1 is important for securing the polarized distribution of membrane lipids at the apical surface and maintenance of apical bile canaliculi in HepG2 cells and hence cell polarity. This study underscores the emerging role of the endosomal recycling system in apical surface development and identifies NHE6 as a novel regulatory protein in this process.",
keywords = "MDCK CELLS, PLASMA-MEMBRANE, SUBAPICAL COMPARTMENT, POLARITY DEVELOPMENT, HEPATIC CELLS, ONCOSTATIN-M, SPHINGOLIPID TRANSPORT, BASOLATERAL PROTEINS, INTRACELLULAR SITES, INCLUSION DISEASE",
author = "Ryuichi Ohgaki and Masafumi Matsushita and Hiroshi Kanazawa and Satoshi Ogihara and Dick Hoekstra and {van IJzendoorn}, {Sven C. D.}",
year = "2010",
month = "4",
day = "1",
doi = "10.1091/mbc.E09-09-0767",
language = "English",
volume = "21",
pages = "1293--1304",
journal = "Molecular Biology of the Cell",
issn = "1059-1524",
publisher = "AMER SOC CELL BIOLOGY",
number = "7",

}

RIS

TY - JOUR

T1 - The Na+/H+ Exchanger NHE6 in the Endosomal Recycling System Is Involved in the Development of Apical Bile Canalicular Surface Domains in HepG2 Cells

AU - Ohgaki, Ryuichi

AU - Matsushita, Masafumi

AU - Kanazawa, Hiroshi

AU - Ogihara, Satoshi

AU - Hoekstra, Dick

AU - van IJzendoorn, Sven C. D.

PY - 2010/4/1

Y1 - 2010/4/1

N2 - Polarized epithelial cells develop and maintain distinct apical and basolateral surface domains despite a continuous flux of membranes between these domains. The Na+/H+ exchanger NHE6 localizes to endosomes but its function is unknown. Here, we demonstrate that polarized hepatoma HepG2 cells express an NHE6.1 variant that localizes to recycling endosomes and colocalizes with transcytosing bulk membrane lipids. NHE6.1 knockdown or overexpression decreases or increases recycling endosome pH, respectively, and inhibits the maintenance of apical, bile canalicular plasma membranes and, concomitantly, apical lumens. NHE6.1 knockdown or overexpression has little effect on the de novo biogenesis of apical surface domains. NHE6.1 knockdown does not inhibit basolateral-to-apical transcytosis of bulk membrane lipids, but it does promote their progressive loss from the apical surface, leaving cells unable to efficiently retain bulk membrane and bile canalicular proteins at the apical surface. The data suggest that a limited range of endosome pH mediated by NHE6.1 is important for securing the polarized distribution of membrane lipids at the apical surface and maintenance of apical bile canaliculi in HepG2 cells and hence cell polarity. This study underscores the emerging role of the endosomal recycling system in apical surface development and identifies NHE6 as a novel regulatory protein in this process.

AB - Polarized epithelial cells develop and maintain distinct apical and basolateral surface domains despite a continuous flux of membranes between these domains. The Na+/H+ exchanger NHE6 localizes to endosomes but its function is unknown. Here, we demonstrate that polarized hepatoma HepG2 cells express an NHE6.1 variant that localizes to recycling endosomes and colocalizes with transcytosing bulk membrane lipids. NHE6.1 knockdown or overexpression decreases or increases recycling endosome pH, respectively, and inhibits the maintenance of apical, bile canalicular plasma membranes and, concomitantly, apical lumens. NHE6.1 knockdown or overexpression has little effect on the de novo biogenesis of apical surface domains. NHE6.1 knockdown does not inhibit basolateral-to-apical transcytosis of bulk membrane lipids, but it does promote their progressive loss from the apical surface, leaving cells unable to efficiently retain bulk membrane and bile canalicular proteins at the apical surface. The data suggest that a limited range of endosome pH mediated by NHE6.1 is important for securing the polarized distribution of membrane lipids at the apical surface and maintenance of apical bile canaliculi in HepG2 cells and hence cell polarity. This study underscores the emerging role of the endosomal recycling system in apical surface development and identifies NHE6 as a novel regulatory protein in this process.

KW - MDCK CELLS

KW - PLASMA-MEMBRANE

KW - SUBAPICAL COMPARTMENT

KW - POLARITY DEVELOPMENT

KW - HEPATIC CELLS

KW - ONCOSTATIN-M

KW - SPHINGOLIPID TRANSPORT

KW - BASOLATERAL PROTEINS

KW - INTRACELLULAR SITES

KW - INCLUSION DISEASE

U2 - 10.1091/mbc.E09-09-0767

DO - 10.1091/mbc.E09-09-0767

M3 - Article

VL - 21

SP - 1293

EP - 1304

JO - Molecular Biology of the Cell

JF - Molecular Biology of the Cell

SN - 1059-1524

IS - 7

ER -

ID: 5063279