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Rapid Cycling of Lipid Raft Markers between the Cell Surface and Golgi Complex

The endocytic itineraries of lipid raft markers, such as glycosyl phosphatidylinositol (GPI)-anchored proteins and glycosphingolipids, are incompletely understood. Here we show that different GPI-anchored proteins have different intracellular distributions; some (such as the folate receptor) accumul...

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Autores principales: Nichols, Benjamin J., Kenworthy, Anne K., Polishchuk, Roman S., Lodge, Robert, Roberts, Theresa H., Hirschberg, Koret, Phair, Robert D., Lippincott-Schwartz, Jennifer
Formato: Texto
Lenguaje:English
Publicado: The Rockefeller University Press 2001
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2190578/
https://www.ncbi.nlm.nih.gov/pubmed/11331304
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author Nichols, Benjamin J.
Kenworthy, Anne K.
Polishchuk, Roman S.
Lodge, Robert
Roberts, Theresa H.
Hirschberg, Koret
Phair, Robert D.
Lippincott-Schwartz, Jennifer
author_facet Nichols, Benjamin J.
Kenworthy, Anne K.
Polishchuk, Roman S.
Lodge, Robert
Roberts, Theresa H.
Hirschberg, Koret
Phair, Robert D.
Lippincott-Schwartz, Jennifer
author_sort Nichols, Benjamin J.
collection PubMed
description The endocytic itineraries of lipid raft markers, such as glycosyl phosphatidylinositol (GPI)-anchored proteins and glycosphingolipids, are incompletely understood. Here we show that different GPI-anchored proteins have different intracellular distributions; some (such as the folate receptor) accumulate in transferrin-containing compartments, others (such as CD59 and GPI-linked green fluorescent protein [GFP]) accumulate in the Golgi apparatus. Selective photobleaching shows that the Golgi pool of both GPI-GFP and CD59-GFP constantly and rapidly exchanges with the pool of these proteins found on the plasma membrane (PM). We visualized intermediates carrying GPI-GFP from the Golgi apparatus to the PM and separate structures delivering GPI-GFP to the Golgi apparatus. GPI-GFP does not accumulate within endocytic compartments containing transferrin, although it is detected in intracellular structures which are endosomes by the criteria of accessibility to a fluid phase marker and to cholera and shiga toxin B subunits (CTxB and STxB, which are also found in rafts). GPI-GFP and a proportion of the total CTxB and STxB taken up into cells are endocytosed independently of clathrin-associated machinery and are delivered to the Golgi complex via indistinguishable mechanisms. Hence, they enter the Golgi complex in the same intermediates, get there independently of both clathrin and rab5 function, and are excluded from it at 20°C and under conditions of cholesterol sequestration. The PM–Golgi cycling pathway followed by GPI-GFP could serve to regulate lipid raft distribution and function within cells.
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spelling pubmed-21905782008-05-01 Rapid Cycling of Lipid Raft Markers between the Cell Surface and Golgi Complex Nichols, Benjamin J. Kenworthy, Anne K. Polishchuk, Roman S. Lodge, Robert Roberts, Theresa H. Hirschberg, Koret Phair, Robert D. Lippincott-Schwartz, Jennifer J Cell Biol Original Article The endocytic itineraries of lipid raft markers, such as glycosyl phosphatidylinositol (GPI)-anchored proteins and glycosphingolipids, are incompletely understood. Here we show that different GPI-anchored proteins have different intracellular distributions; some (such as the folate receptor) accumulate in transferrin-containing compartments, others (such as CD59 and GPI-linked green fluorescent protein [GFP]) accumulate in the Golgi apparatus. Selective photobleaching shows that the Golgi pool of both GPI-GFP and CD59-GFP constantly and rapidly exchanges with the pool of these proteins found on the plasma membrane (PM). We visualized intermediates carrying GPI-GFP from the Golgi apparatus to the PM and separate structures delivering GPI-GFP to the Golgi apparatus. GPI-GFP does not accumulate within endocytic compartments containing transferrin, although it is detected in intracellular structures which are endosomes by the criteria of accessibility to a fluid phase marker and to cholera and shiga toxin B subunits (CTxB and STxB, which are also found in rafts). GPI-GFP and a proportion of the total CTxB and STxB taken up into cells are endocytosed independently of clathrin-associated machinery and are delivered to the Golgi complex via indistinguishable mechanisms. Hence, they enter the Golgi complex in the same intermediates, get there independently of both clathrin and rab5 function, and are excluded from it at 20°C and under conditions of cholesterol sequestration. The PM–Golgi cycling pathway followed by GPI-GFP could serve to regulate lipid raft distribution and function within cells. The Rockefeller University Press 2001-04-30 /pmc/articles/PMC2190578/ /pubmed/11331304 Text en © 2001 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 Original Article
Nichols, Benjamin J.
Kenworthy, Anne K.
Polishchuk, Roman S.
Lodge, Robert
Roberts, Theresa H.
Hirschberg, Koret
Phair, Robert D.
Lippincott-Schwartz, Jennifer
Rapid Cycling of Lipid Raft Markers between the Cell Surface and Golgi Complex
title Rapid Cycling of Lipid Raft Markers between the Cell Surface and Golgi Complex
title_full Rapid Cycling of Lipid Raft Markers between the Cell Surface and Golgi Complex
title_fullStr Rapid Cycling of Lipid Raft Markers between the Cell Surface and Golgi Complex
title_full_unstemmed Rapid Cycling of Lipid Raft Markers between the Cell Surface and Golgi Complex
title_short Rapid Cycling of Lipid Raft Markers between the Cell Surface and Golgi Complex
title_sort rapid cycling of lipid raft markers between the cell surface and golgi complex
topic Original Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2190578/
https://www.ncbi.nlm.nih.gov/pubmed/11331304
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