MAL2, a novel raft protein of the MAL family, is an essential component of the machinery for transcytosis in hepatoma HepG2 cells
Transcytosis is used alone (e.g., hepatoma HepG2 cells) or in combination with a direct pathway from the Golgi (e.g., epithelial MDCK cells) as an indirect route for targeting proteins to the apical surface. The raft-associated MAL protein is an essential element of the machinery for the direct rout...
Autores principales: | , , , , , , , , |
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Formato: | Texto |
Lenguaje: | English |
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The Rockefeller University Press
2002
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Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2173496/ https://www.ncbi.nlm.nih.gov/pubmed/12370246 http://dx.doi.org/10.1083/jcb.200206033 |
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author | de Marco, María C. Martín-Belmonte, Fernando Kremer, Leonor Albar, Juan P. Correas, Isabel Vaerman, Jean P. Marazuela, Mónica Byrne, Jennifer A. Alonso, Miguel A. |
author_facet | de Marco, María C. Martín-Belmonte, Fernando Kremer, Leonor Albar, Juan P. Correas, Isabel Vaerman, Jean P. Marazuela, Mónica Byrne, Jennifer A. Alonso, Miguel A. |
author_sort | de Marco, María C. |
collection | PubMed |
description | Transcytosis is used alone (e.g., hepatoma HepG2 cells) or in combination with a direct pathway from the Golgi (e.g., epithelial MDCK cells) as an indirect route for targeting proteins to the apical surface. The raft-associated MAL protein is an essential element of the machinery for the direct route in MDCK cells. Herein, we present the functional characterization of MAL2, a member of the MAL protein family, in polarized HepG2 cells. MAL2 resided selectively in rafts and is predominantly distributed in a compartment localized beneath the subapical F-actin cytoskeleton. MAL2 greatly colocalized in subapical endosome structures with transcytosing molecules en route to the apical surface. Depletion of endogenous MAL2 drastically blocked transcytotic transport of exogenous polymeric immunoglobulin receptor and endogenous glycosylphosphatidylinositol-anchored protein CD59 to the apical membrane. MAL2 depletion did not affect the internalization of these molecules but produced their accumulation in perinuclear endosome elements that were accessible to transferrin. Normal transcytosis persisted in cells that expressed exogenous MAL2 designed to resist the depletion treatment. MAL2 is therefore essential for transcytosis in HepG2 cells. |
format | Text |
id | pubmed-2173496 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2002 |
publisher | The Rockefeller University Press |
record_format | MEDLINE/PubMed |
spelling | pubmed-21734962008-05-01 MAL2, a novel raft protein of the MAL family, is an essential component of the machinery for transcytosis in hepatoma HepG2 cells de Marco, María C. Martín-Belmonte, Fernando Kremer, Leonor Albar, Juan P. Correas, Isabel Vaerman, Jean P. Marazuela, Mónica Byrne, Jennifer A. Alonso, Miguel A. J Cell Biol Report Transcytosis is used alone (e.g., hepatoma HepG2 cells) or in combination with a direct pathway from the Golgi (e.g., epithelial MDCK cells) as an indirect route for targeting proteins to the apical surface. The raft-associated MAL protein is an essential element of the machinery for the direct route in MDCK cells. Herein, we present the functional characterization of MAL2, a member of the MAL protein family, in polarized HepG2 cells. MAL2 resided selectively in rafts and is predominantly distributed in a compartment localized beneath the subapical F-actin cytoskeleton. MAL2 greatly colocalized in subapical endosome structures with transcytosing molecules en route to the apical surface. Depletion of endogenous MAL2 drastically blocked transcytotic transport of exogenous polymeric immunoglobulin receptor and endogenous glycosylphosphatidylinositol-anchored protein CD59 to the apical membrane. MAL2 depletion did not affect the internalization of these molecules but produced their accumulation in perinuclear endosome elements that were accessible to transferrin. Normal transcytosis persisted in cells that expressed exogenous MAL2 designed to resist the depletion treatment. MAL2 is therefore essential for transcytosis in HepG2 cells. The Rockefeller University Press 2002-10-14 /pmc/articles/PMC2173496/ /pubmed/12370246 http://dx.doi.org/10.1083/jcb.200206033 Text en Copyright © 2002, The Rockefeller University Press This article is distributed under the terms of an Attribution–Noncommercial–Share Alike–No Mirror Sites license for the first six months after the publication date (see http://www.rupress.org/terms). After six months it is available under a Creative Commons License (Attribution–Noncommercial–Share Alike 4.0 Unported license, as described at http://creativecommons.org/licenses/by-nc-sa/4.0/). |
spellingShingle | Report de Marco, María C. Martín-Belmonte, Fernando Kremer, Leonor Albar, Juan P. Correas, Isabel Vaerman, Jean P. Marazuela, Mónica Byrne, Jennifer A. Alonso, Miguel A. MAL2, a novel raft protein of the MAL family, is an essential component of the machinery for transcytosis in hepatoma HepG2 cells |
title | MAL2, a novel raft protein of the MAL family, is an essential component of the machinery for transcytosis in hepatoma HepG2 cells |
title_full | MAL2, a novel raft protein of the MAL family, is an essential component of the machinery for transcytosis in hepatoma HepG2 cells |
title_fullStr | MAL2, a novel raft protein of the MAL family, is an essential component of the machinery for transcytosis in hepatoma HepG2 cells |
title_full_unstemmed | MAL2, a novel raft protein of the MAL family, is an essential component of the machinery for transcytosis in hepatoma HepG2 cells |
title_short | MAL2, a novel raft protein of the MAL family, is an essential component of the machinery for transcytosis in hepatoma HepG2 cells |
title_sort | mal2, a novel raft protein of the mal family, is an essential component of the machinery for transcytosis in hepatoma hepg2 cells |
topic | Report |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2173496/ https://www.ncbi.nlm.nih.gov/pubmed/12370246 http://dx.doi.org/10.1083/jcb.200206033 |
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